1593:. Through mitochondrial fission, a number of daughter mitochondria are created, often with an uneven distribution in membrane potential. Mitochondria with a strong, healthy membrane potential were more likely to undergo fusion than mitochondria with low membrane potential. Interference with the mitochondrial fission pathway led to an increase in oxidized proteins and a decrease in respiration. Without PINK1, parkin cannot efficiently localize to damaged mitochondria, while an over-expression of PINK1 causes parkin to localize to even healthy mitochondria. Furthermore, mutations in both Drp1, a mitochondrial fission factor, and PINK1 were fatal in
1569:
244:
221:
118:
143:
1578:
502:
495:
250:
149:
1561:. Healthy mitochondria maintain a membrane potential that can be used to import PINK1 into the inner membrane where it is cleaved by PARL and cleared from the outer membrane. Severely damaged mitochondria lack sufficient membrane potential to import PINK1, which then accumulates on the outer membrane. PINK1 then recruits parkin to target the damaged mitochondria for degradation through
1643:
was shown by others that the nucleoside derivative of kinetin, i.e. kinetin riboside, exhibited significant activation of PINK1 in cells. Additionally, the monophosphate prodrugs of kinetin riboside, ProTides, also showed activation of PINK1. In
December 2017, niclosamide, an anthelmintic drug, was identified as a potent activator of PINK1 in cells and in neurons.
1630:. Mutations in the PINK1 protein have been shown to lead to a build-up of such improperly folded proteins in the mitochondria of both fly and human cells. Specifically, mutations in the serine/threonine kinase domain have been found in a number of Parkinson's patients where PINK1 fails to protect against stress-induced mitochondrial dysfunction and
3262:
Rogaeva E, Johnson J, Lang AE, Gulick C, Gwinn-Hardy K, Kawarai T, Sato C, Morgan A, Werner J, Nussbaum R, Petit A, Okun MS, McInerney A, Mandel R, Groen JL, Fernandez HH, Postuma R, Foote KD, Salehi-Rad S, Liang Y, Reimsnider S, Tandon A, Hardy J, St George-Hyslop P, Singleton AB (2005). "Analysis
1642:
To date, there have been few reports of small molecules that activate PINK1 and their promise as potential treatments for
Parkinson's disease. The first report appeared in 2013 when Kevan Shokat and his team from UCSF identified a nucleobase called kinetin as an activator of PINK1. Subsequently, it
3187:
Hatano Y, Sato K, Elibol B, Yoshino H, Yamamura Y, Bonifati V, Shinotoh H, Asahina M, Kobayashi S, Ng AR, Rosales RL, Hassin-Baer S, Shinar Y, Lu CS, Chang HC, Wu-Chou YH, Ataç FB, Kobayashi T, Toda T, Mizuno Y, Hattori N (2004). "PARK6-linked autosomal recessive early-onset parkinsonism in Asian
2954:
Bonifati V, Dekker MC, Vanacore N, Fabbrini G, Squitieri F, Marconi R, Antonini A, Brustenghi P, Dalla Libera A, De Mari M, Stocchi F, Montagna P, Gallai V, Rizzu P, van
Swieten JC, Oostra B, van Duijn CM, Meco G, Heutink P (2003). "Autosomal recessive early onset parkinsonism is linked to three
1601:
In addition to mitochondrial fission, PINK1 has been implicated in mitochondrial motility. The accumulation of PINK1 and recruitment of parkin targets a mitochondrion for degradation, and PINK1 may serve to enhance degradation rates by arresting mitochondrial motility. Over-expression of PINK1
1609:
Another mechanism of mitochondrial quality control may arise through mitochondria-derived vesicles. Oxidative stress in mitochondria can produce potentially harmful compounds including improperly folded proteins or reactive oxygen species. PINK1 has been shown to facilitate the creation of
2992:
Valente EM, Brancati F, Caputo V, Graham EA, Davis MB, Ferraris A, Breteler MM, Gasser T, Bonifati V, Bentivoglio AR, De
Michele G, Dürr A, Cortelli P, Filla A, Meco G, Oostra BA, Brice A, Albanese A, Dallapiccola B, Wood NW (2003). "PARK6 is a common cause of familial parkinsonism".
1545:
regulatory sequence. The protein has been found to localize to the outer membrane of mitochondria, but can also be found throughout the cytosol. Experiments suggest the Ser/Thr kinase domain faces outward toward the cytosol, indicating a possible point of interaction with parkin.
3059:
Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG, Albanese A, Nussbaum R, González-Maldonado R, Deller T, Salvi S, Cortelli P, Gilks WP, Latchman DS, Harvey RJ, Dallapiccola B, Auburger G, Wood NW (2004).
2561:
Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG, Albanese A, Nussbaum R, González-Maldonado R, Deller T, Salvi S, Cortelli P, Gilks WP, Latchman DS, Harvey RJ, Dallapiccola B, Auburger G, Wood NW (2004).
3149:
Hatano Y, Li Y, Sato K, Asakawa S, Yamamura Y, Tomiyama H, Yoshino H, Asahina M, Kobayashi S, Hassin-Baer S, Lu CS, Ng AR, Rosales RL, Shimizu N, Toda T, Mizuno Y, Hattori N (2004). "Novel PINK1 mutations in early-onset parkinsonism".
3388:
Li Y, Tomiyama H, Sato K, Hatano Y, Yoshino H, Atsumi M, Kitaguchi M, Sasaki S, Kawaguchi S, Miyajima H, Toda T, Mizuno Y, Hattori N (2005). "Clinicogenetic study of PINK1 mutations in autosomal recessive early-onset parkinsonism".
3111:
Healy DG, Abou-Sleiman PM, Ahmadi KR, Muqit MM, Bhatia KP, Quinn NP, Lees AJ, Latchmann DS, Goldstein DB, Wood NW (2004). "The gene responsible for PARK6 Parkinson's disease, PINK1, does not influence common forms of parkinsonism".
1572:
Damaged mitochondria is being recognized by PINK1. PINK1 builds up on the outer membrane of the mitochondria and recruits parkin. The PINK1/parkin pathway then designates the mitochondria for degradation by
1597:
models. However, an over-expression of Drp1 could rescue subjects deficient in PINK1 or parkin, suggesting mitochondrial fission initiated by Drp1 recreates the same effects of the PINK1/parkin pathway.
1778:
Valente EM, Salvi S, Ialongo T, Marongiu R, Elia AE, Caputo V, Romito L, Albanese A, Dallapiccola B, Bentivoglio AR (Sep 2004). "PINK1 mutations are associated with sporadic early-onset parkinsonism".
2917:
Khan NL, Valente EM, Bentivoglio AR, Wood NW, Albanese A, Brooks DJ, Piccini P (2002). "Clinical and subclinical dopaminergic dysfunction in PARK6-linked parkinsonism: an 18F-dopa PET study".
1513:
of those mitochondria. PINK1 is processed by healthy mitochondria and released to trigger neuron differentiation. Mutations in this gene cause one form of autosomal recessive early-onset
2302:
Vives-Bauza C, Zhou C, Huang Y, Cui M, de Vries RL, Kim J, May J, Tocilescu MA, Liu W, Ko HS, Magrané J, Moore DJ, Dawson VL, Grailhe R, Dawson TM, Li C, Tieu K, Przedborski S (2010).
3030:
Nakajima A, Kataoka K, Hong M, Sakaguchi M, Huh NH (2004). "BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential".
2253:
Twig G, Elorza A, Molina AJ, Mohamed H, Wikstrom JD, Walzer G, Stiles L, Haigh SE, Katz S, Las G, Alroy J, Wu M, Py BF, Yuan J, Deeney JT, Corkey BE, Shirihai OS (2008).
257:
156:
3225:
Healy DG, Abou-Sleiman PM, Gibson JM, Ross OA, Jain S, Gandhi S, Gosal D, Muqit MM, Wood NW, Lynch T (2006). "PINK1 (PARK6) associated
Parkinson disease in Ireland".
2719:"Kinetin Riboside and Its ProTides Activate the Parkinson's Disease Associated PTEN-Induced Putative Kinase 1 (PINK1) Independent of Mitochondrial Depolarization"
2670:"Kinetin Riboside and Its ProTides Activate the Parkinson's Disease Associated PTEN-Induced Putative Kinase 1 (PINK1) Independent of Mitochondrial Depolarization"
1215:
1196:
79:
1565:. Due to the presence of PINK1 throughout the cytoplasm, it has been suggested that PINK1 functions as a "scout" to probe for damaged mitochondria.
1485:
2836:
1719:
1701:
3451:
2766:
Barini E, Miccoli A, Tinarelli F, Mulholand K, Kadri H, Khanim F, Stojanovski L, Read KD, Burness K, Blow JJ, Mehellou Y, Muqit M (2017).
1990:
Deas E, Plun-Favreau H, Gandhi S, Desmond H, Kjaer S, Loh SH, Renton AE, Harvey RJ, Whitworth AJ, Martins LM, Abramov AY, Wood NW (2011).
2412:
Liu S, Sawada T, Lee S, Yu W, Silverio G, Alapatt P, Millan I, Shen A, Saxton W, Kanao T, Takahashi R, Hattori N, Imai Y, Lu B (2012).
243:
1422:
1415:
3294:"Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability"
220:
1976:
2717:
Osgerby L, Lai YC, Thornton PJ, Amalfitano J, Le Duff CS, Jabeen I, Kadri H, Miccoli A, Tucker JH, Muqit M, Mehellou Y (2017).
2668:
Osgerby L, Lai YC, Thornton PJ, Amalfitano J, Le Duff CS, Jabeen I, Kadri H, Miccoli A, Tucker JH, Muqit M, Mehellou Y (2017).
1688:
1667:
1684:
142:
117:
1663:
59:
1568:
2768:"The Anthelmintic Drug Niclosamide and its Analogues Activate the Parkinson's Disease Associated Protein Kinase PINK1"
2876:"Localization of a Novel Locus for Autosomal Recessive Early-Onset Parkinsonism, PARK6, on Human Chromosome 1p35-p36"
256:
155:
1549:
The structure of PINK1 has been solved and shows how the protein binds and phosphorylates its substrate ubiquitin.
249:
148:
2512:
Pimenta de Castro I, Costa AC, Lam D, Tufi R, Fedele V, Moisoi N, Dinsdale D, Deas E, Loh SH, Martins LM (2012).
2414:"Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria"
1260:
67:
3436:
1880:
1241:
2082:
Schubert AF, Gladkova C, Pardon E, Wagstaff JL, Freund SM, Steyaert J, Maslen SL, Komander D (2017-10-30).
1533:, between the 103-Alanine and the 104-Phenylalanine residues, into a 53000 Da fragment. PINK1 contains an
1514:
2465:"Parkin and PINK 1 function in a vesicular trafficking pathway regulating mitochondrial quality control"
1590:
1557:
PINK1 is intimately involved with mitochondrial quality control by identifying damaged mitochondria and
1538:
3305:
3073:
2874:
Valente EM, Bentivoglio AR, Dixon PH, Ferraris A, Ialongo T, Frontali M, Albanese A, Wood NW (2001).
2575:
2315:
2160:
2095:
131:
46:
1623:
1577:
1876:"PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding"
3414:
3376:
3250:
3213:
3175:
3137:
3099:
3018:
2980:
2942:
2854:
2601:
2064:
1803:
1610:
mitochondria-derived vesicles which can separate reactive oxygen species and shuttle them toward
91:
1398:
1377:
1351:
1330:
2621:"A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1"
1739:"Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway"
3406:
3368:
3333:
3280:
3242:
3205:
3167:
3129:
3091:
3047:
3010:
2972:
2934:
2905:
2842:
2832:
2797:
2748:
2699:
2650:
2593:
2543:
2494:
2445:
2394:
2343:
2284:
2235:
2186:
2129:
2111:
2056:
2021:
1958:
1907:
1856:
1795:
1760:
501:
494:
39:
2819:
Heutink P (2006). "PINK-1 and DJ-1 — new genes for autosomal recessive
Parkinson's disease".
1106:
positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization
896:
negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
881:
negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway
3398:
3358:
3323:
3313:
3272:
3234:
3197:
3159:
3121:
3081:
3039:
3002:
2964:
2926:
2895:
2887:
2824:
2787:
2779:
2738:
2730:
2689:
2681:
2640:
2632:
2583:
2533:
2525:
2484:
2476:
2435:
2425:
2384:
2374:
2333:
2323:
2274:
2266:
2255:"Fission and selective fusion govern mitochondrial segregation and elimination by autophagy"
2225:
2217:
2176:
2168:
2119:
2103:
2048:
2011:
2003:
1948:
1940:
1897:
1889:
1846:
1836:
1787:
1750:
1526:
336:
267:
211:
166:
3292:
Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA, Cookson MR (2005).
87:
2866:
1925:
Dagda RK, Pien I, Wang R, Zhu J, Wang KZ, Callio J, Banerjee TD, Dagda RY, Chu CT (2013).
1503:
311:
1821:
Narendra DP, Jin SM, Tanaka A, Suen DF, Gautier CA, Shen J, Cookson MR, Youle RJ (2010).
3309:
3077:
2579:
2319:
2164:
2099:
3402:
3238:
3201:
2900:
2875:
2792:
2767:
2743:
2718:
2694:
2669:
2645:
2620:
2538:
2513:
2489:
2464:
2440:
2413:
2389:
2362:
2338:
2303:
2279:
2254:
2230:
2205:
2181:
2148:
2124:
2083:
2016:
1991:
1953:
1927:"Beyond the mitochondrion: cytosolic PINK1 remodels dendrites through protein kinase A"
1926:
1902:
1875:
1851:
1822:
1603:
3328:
3293:
3043:
1130:
1125:
1120:
1115:
1110:
1105:
1100:
1095:
1090:
1085:
1080:
1075:
1070:
1065:
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1055:
1050:
1045:
1040:
1035:
1030:
1025:
1020:
1015:
1010:
1005:
1000:
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990:
985:
980:
975:
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965:
960:
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950:
945:
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935:
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905:
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865:
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835:
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815:
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629:
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593:
588:
583:
578:
573:
568:
563:
558:
553:
548:
543:
3445:
3363:
3346:
1585:. This prevents any buildup of PINK1 and parkin is not recruited to the mitochondria.
1499:
530:
3418:
3380:
3254:
3217:
3179:
3103:
3022:
2984:
2619:
Hertz NT, Berthet A, Sos ML, Thorn KS, Burlingame AL, Nakamura K, Shokat KM (2013).
2605:
2068:
2039:
Springer W, Kahle PJ (March 2011). "Regulation of PINK1-Parkin-mediated mitophagy".
1807:
71:
3141:
2946:
2206:"Mitochondrail quality control mediated by PINK1 and Parkin: links to parkinsonism"
1827:
329:
108:
1537:
mitochondrial localization sequence, a putative transmembrane sequence, a Ser/Thr
2828:
2734:
2685:
2514:"Genetic analysis of mitochondrial protein misfolding in Drosophila melanogaster"
2430:
1841:
95:
3276:
2221:
1931:
1724:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1706:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1627:
1475:
2636:
2367:
Proceedings of the
National Academy of Sciences of the United States of America
2361:
Poole AC, Thomas RE, Andrews LA, McBride HM, Whitworth AJ, Pallanck LJ (2008).
2308:
Proceedings of the
National Academy of Sciences of the United States of America
412:
1594:
1542:
1534:
228:
125:
75:
3347:"G309D and W437OPA PINK1 mutations in Caucasian Parkinson's disease patients"
2823:. Journal of Neural Transmission. Supplementa. Vol. 70. pp. 215–9.
2270:
2115:
1823:"PINK1 is selectively stabilized on impaired mitochondria to activate Parkin"
3437:
GeneReviews/NCBI/NIH/UW entry on PINK1 Type of Young-Onset Parkinson Disease
3318:
3086:
3061:
2588:
2563:
2379:
2328:
2172:
1631:
1611:
1562:
1558:
1510:
1160:
906:
negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
751:
positive regulation of mitophagy in response to mitochondrial depolarization
472:
350:
295:
282:
194:
181:
83:
3410:
3372:
3337:
3284:
3246:
3209:
3171:
3133:
3095:
3051:
3014:
2976:
2938:
2909:
2846:
2801:
2783:
2752:
2703:
2654:
2597:
2547:
2498:
2480:
2449:
2398:
2347:
2288:
2239:
2190:
2133:
2060:
2052:
2025:
1962:
1911:
1860:
1799:
1764:
1755:
1738:
861:
positive regulation of mitochondrial electron transport, NADH to ubiquinone
3006:
2968:
1893:
1581:
Healthy mitochondria can import PINK1 where it is subsequently cleaved by
1462:
1457:
3062:"Hereditary early-onset Parkinson's disease caused by mutations in PINK1"
2564:"Hereditary early-onset Parkinson's disease caused by mutations in PINK1"
2007:
1446:
1305:
1286:
2107:
2529:
1506:
1272:
1227:
3263:
of the PINK1 gene in a large cohort of cases with Parkinson disease".
3163:
3125:
2930:
1944:
1874:
Lazarou M, Narendra DP, Jin SM, Tekle E, Banerjee S, Youle RJ (2013).
1791:
1430:
1182:
2304:"PINK1-dependent recruitment of Parkin to mitochondria in mitophagy"
1992:"PINK1 cleavage at position A103 by the mitochondrial protease PARL"
50:, BRPK, PARK6, PTEN induced putative kinase 1, PTEN induced kinase 1
2891:
1626:
and associated with the build-up of improperly folded proteins and
1622:
Parkinson's disease is often characterized by the degeneration of
1576:
1567:
1145:
1141:
2463:
McLelland GL, Soubannier V, Chen CX, McBride HM, Fon EA (2014).
1582:
1530:
1492:
1066:
negative regulation of reactive oxygen species metabolic process
971:
positive regulation of release of cytochrome c from mitochondria
941:
positive regulation of DNA-binding transcription factor activity
510:
63:
1606:, a protein closely associated with mitochondrial migration.
876:
positive regulation of ubiquitin-protein transferase activity
2363:"The PINK1/Parkin pathway regulates mitochondrial mitophagy"
2084:"Structure of PINK1 in complex with its substrate ubiquitin"
1131:
negative regulation of intrinsic apoptotic signaling pathway
926:
negative regulation of oxidative stress-induced neuron death
1056:
positive regulation of I-kappaB kinase/NF-kappaB signaling
901:
positive regulation of synaptic transmission, dopaminergic
891:
negative regulation of oxidative stress-induced cell death
756:
positive regulation of free ubiquitin chain polymerization
1006:
positive regulation of protein targeting to mitochondrion
319:
1126:
positive regulation of NMDA glutamate receptor activity
951:
regulation of reactive oxygen species metabolic process
1041:
establishment of protein localization to mitochondrion
851:
positive regulation of peptidyl-serine phosphorylation
484:
1589:
PINK1 may also control mitochondria quality through
3345:Deng H, Le WD, Zhang X, Pan TH, Jankovic J (2005).
1977:"Entrez Gene: PINK1 PTEN induced putative kinase 1"
1498:It is thought to protect cells from stress-induced
1391:
1370:
1344:
1323:
1091:
regulation of cellular response to oxidative stress
1081:
positive regulation of histone deacetylase activity
986:
regulation of proteasomal protein catabolic process
1680:
1678:
1676:
1659:
1657:
1655:
675:integral component of mitochondrial outer membrane
946:negative regulation of autophagy of mitochondrion
921:regulation of hydrogen peroxide metabolic process
816:positive regulation of protein kinase B signaling
801:regulation of protein-containing complex assembly
266:
165:
966:regulation of protein targeting to mitochondrion
961:maintenance of protein location in mitochondrion
821:positive regulation of protein dephosphorylation
705:mitochondrial outer membrane translocase complex
1559:targeting specific mitochondria for degradation
956:positive regulation of ATP biosynthetic process
746:negative regulation of neuron apoptotic process
16:Protein-coding gene in the species Homo sapiens
1685:GRCm38: Ensembl release 89: ENSMUSG00000028756
1509:to bind to depolarized mitochondria to induce
1076:positive regulation of protein phosphorylation
1026:regulation of mitochondrial membrane potential
771:positive regulation of catecholamine secretion
981:positive regulation of protein ubiquitination
826:ubiquitin-dependent protein catabolic process
811:negative regulation of autophagosome assembly
8:
1101:positive regulation of mitochondrial fission
856:negative regulation of mitochondrial fission
2149:"Mitochondrial fission, fusion, and stress"
1664:GRCh38: Ensembl release 89: ENSG00000158828
2210:Cold Spring Harbor Perspectives in Biology
1156:
526:
307:
206:
103:
3362:
3327:
3317:
3085:
2899:
2821:Parkinson's Disease and Related Disorders
2791:
2742:
2693:
2644:
2587:
2537:
2488:
2439:
2429:
2388:
2378:
2337:
2327:
2278:
2229:
2180:
2123:
2015:
1952:
1901:
1850:
1840:
1754:
1016:positive regulation of peptidase activity
791:positive regulation of dopamine secretion
574:calcium-dependent protein kinase activity
1071:negative regulation of apoptotic process
1011:positive regulation of cristae formation
916:regulation of mitochondrion organization
871:regulation of autophagy of mitochondrion
776:regulation of synaptic vesicle transport
569:protein serine/threonine kinase activity
2204:Narendra D, Walker JE, Youle R (2012).
1651:
1502:dysfunction. PINK1 activity causes the
991:activation of protein kinase B activity
911:regulation of oxidative phosphorylation
2862:
2852:
1602:produced similar effects to silencing
846:negative regulation of gene expression
836:regulation of neuron apoptotic process
20:
1111:cellular response to hydrogen sulfide
1061:cellular response to oxidative stress
1001:negative regulation of macroautophagy
866:positive regulation of macroautophagy
544:C3HC4-type RING finger domain binding
271:
232:
227:
170:
129:
124:
7:
976:respiratory electron transport chain
766:cellular response to toxic substance
761:regulation of protein ubiquitination
2147:Youle RJ, van der Bliek AM (2012).
1121:negative regulation of neuron death
1086:mitochondrion to lysosome transport
831:peptidyl-serine autophosphorylation
3403:10.1212/01.WNL.0000164009.36740.4E
3239:10.1212/01.wnl.0000142089.38301.8e
3202:10.1212/01.wnl.0000142258.29304.fe
1529:protein which is often cleaved by
1388:
1367:
1341:
1320:
1296:
1277:
1251:
1232:
1206:
1187:
1036:negative regulation of JNK cascade
781:positive regulation of translation
489:
407:
345:
324:
14:
996:intracellular signal transduction
645:mitochondrial intermembrane space
3364:10.1111/j.1600-0404.2005.00383.x
2955:loci: PARK2, PARK6, and PARK7".
2518:Cell Death & Differentiation
1737:Unoki M, Nakamura Y (Aug 2001).
1525:PINK1 is synthesized as a 63000
614:ubiquitin protein ligase binding
500:
493:
255:
248:
242:
219:
154:
147:
141:
116:
1486:serine/threonine-protein kinase
1051:peptidyl-serine phosphorylation
655:perinuclear region of cytoplasm
695:integral component of membrane
511:More reference expression data
473:More reference expression data
1:
3044:10.1016/S0304-3835(03)00443-9
240:
139:
3298:Proc. Natl. Acad. Sci. U.S.A
2829:10.1007/978-3-211-45295-0_33
2735:10.1021/acs.jmedchem.6b01897
2686:10.1021/acs.jmedchem.6b01897
2431:10.1371/journal.pgen.1002537
1842:10.1371/journal.pbio.1000298
1638:Pharmacological manipulation
841:response to oxidative stress
806:cellular response to hypoxia
725:mitochondrial inner membrane
680:mitochondrial outer membrane
579:peptidase activator activity
3452:Genes on human chromosome 1
3277:10.1001/archneur.61.12.1898
2222:10.1101/cshperspect.a011338
3468:
2637:10.1016/j.cell.2013.07.030
1046:autophagy of mitochondrion
936:mitochondrion organization
451:sternocleidomastoid muscle
1720:"Mouse PubMed Reference:"
1702:"Human PubMed Reference:"
1461:
1456:
1452:
1445:
1429:
1423:Chr 4: 138.04 – 138.05 Mb
1410:
1395:
1374:
1363:
1348:
1327:
1316:
1303:
1299:
1284:
1280:
1271:
1258:
1254:
1239:
1235:
1226:
1213:
1209:
1194:
1190:
1181:
1166:
1159:
1155:
1139:
529:
525:
508:
492:
483:
470:
419:
410:
357:
348:
318:
310:
306:
289:
276:
239:
218:
209:
205:
188:
175:
138:
115:
106:
102:
57:
54:
44:
37:
32:
28:
23:
2271:10.1038/sj.emboj.7601963
700:ubiquitin ligase complex
609:protein kinase B binding
361:tendon of biceps brachii
3319:10.1073/pnas.0500617102
3087:10.1126/science.1096284
2589:10.1126/science.1096284
2380:10.1073/pnas.0709336105
2329:10.1073/pnas.0911187107
2173:10.1126/science.1219855
1881:Journal of Cell Biology
1416:Chr 1: 20.63 – 20.65 Mb
786:protein phosphorylation
559:protein kinase activity
427:myocardium of ventricle
2784:10.1002/cbic.201700500
2481:10.1002/embj.201385902
2053:10.4161/auto.7.3.14348
1756:10.1038/sj.onc.1204608
1586:
1574:
886:protein ubiquitination
443:triceps brachii muscle
3265:Archives of Neurology
3007:10.1007/s100720200097
2969:10.1007/s100720200069
1894:10.1083/jcb.201210111
1591:mitochondrial fission
1580:
1571:
1484:) is a mitochondrial
931:protein stabilization
584:magnesium ion binding
1624:dopaminergic neurons
1096:response to ischemia
710:astrocyte projection
589:transferase activity
369:gastrocnemius muscle
234:Chromosome 4 (mouse)
132:Chromosome 1 (human)
3310:2005PNAS..102.5703B
3078:2004Sci...304.1158V
3001:(Suppl 2): S117–8.
2963:(Suppl 2): S59–60.
2580:2004Sci...304.1158V
2320:2010PNAS..107..378V
2165:2012Sci...337.1062Y
2159:(6098): 1062–1065.
2108:10.1038/nature24645
2100:2017Natur.552...51S
1515:Parkinson's disease
3351:Acta Neurol. Scand
2530:10.1038/cdd.2012.5
2008:10.1093/hmg/ddq526
1587:
1575:
1261:ENSMUSG00000028756
739:Biological process
623:Cellular component
604:nucleotide binding
537:Molecular function
459:extraocular muscle
431:intercostal muscle
373:right frontal lobe
3164:10.1002/ana.20251
3126:10.1002/ana.20206
3072:(5674): 1158–60.
2931:10.1002/ana.10417
2880:Am. J. Hum. Genet
2838:978-3-211-28927-3
2574:(5674): 1158–60.
1945:10.1111/jnc.12494
1792:10.1002/ana.20256
1618:Disease relevance
1614:for degradation.
1478:-induced kinase 1
1472:
1471:
1468:
1467:
1441:
1440:
1406:
1405:
1385:
1384:
1359:
1358:
1338:
1337:
1312:
1311:
1293:
1292:
1267:
1266:
1248:
1247:
1222:
1221:
1203:
1202:
1151:
1150:
564:metal ion binding
521:
520:
517:
516:
479:
478:
466:
465:
404:
403:
397:nucleus accumbens
377:prefrontal cortex
302:
301:
201:
200:
96:PINK1 - orthologs
3459:
3422:
3384:
3366:
3341:
3331:
3321:
3288:
3271:(12): 1898–904.
3258:
3221:
3183:
3145:
3107:
3089:
3055:
3026:
2988:
2950:
2913:
2903:
2870:
2864:
2860:
2858:
2850:
2806:
2805:
2795:
2763:
2757:
2756:
2746:
2714:
2708:
2707:
2697:
2665:
2659:
2658:
2648:
2616:
2610:
2609:
2591:
2558:
2552:
2551:
2541:
2509:
2503:
2502:
2492:
2469:The EMBO Journal
2460:
2454:
2453:
2443:
2433:
2409:
2403:
2402:
2392:
2382:
2358:
2352:
2351:
2341:
2331:
2299:
2293:
2292:
2282:
2259:The EMBO Journal
2250:
2244:
2243:
2233:
2201:
2195:
2194:
2184:
2144:
2138:
2137:
2127:
2079:
2073:
2072:
2036:
2030:
2029:
2019:
1987:
1981:
1980:
1973:
1967:
1966:
1956:
1922:
1916:
1915:
1905:
1871:
1865:
1864:
1854:
1844:
1818:
1812:
1811:
1775:
1769:
1768:
1758:
1734:
1728:
1727:
1716:
1710:
1709:
1698:
1692:
1682:
1671:
1661:
1454:
1453:
1425:
1418:
1401:
1389:
1380:
1368:
1364:RefSeq (protein)
1354:
1342:
1333:
1321:
1297:
1278:
1252:
1233:
1207:
1188:
1157:
594:protease binding
527:
513:
504:
497:
490:
475:
439:digastric muscle
415:
413:Top expressed in
408:
353:
351:Top expressed in
346:
325:
308:
298:
285:
274:
259:
252:
246:
235:
223:
207:
197:
184:
173:
158:
151:
145:
134:
120:
104:
98:
49:
42:
21:
3467:
3466:
3462:
3461:
3460:
3458:
3457:
3456:
3442:
3441:
3433:
3427:
3425:
3387:
3344:
3291:
3261:
3224:
3186:
3148:
3110:
3058:
3029:
2991:
2953:
2916:
2873:
2861:
2851:
2839:
2818:
2814:
2812:Further reading
2809:
2765:
2764:
2760:
2716:
2715:
2711:
2667:
2666:
2662:
2618:
2617:
2613:
2560:
2559:
2555:
2511:
2510:
2506:
2462:
2461:
2457:
2411:
2410:
2406:
2360:
2359:
2355:
2301:
2300:
2296:
2252:
2251:
2247:
2216:(11): a011338.
2203:
2202:
2198:
2146:
2145:
2141:
2094:(7683): 51–56.
2081:
2080:
2076:
2038:
2037:
2033:
1996:Hum. Mol. Genet
1989:
1988:
1984:
1975:
1974:
1970:
1924:
1923:
1919:
1873:
1872:
1868:
1835:(1): e1000298.
1820:
1819:
1815:
1777:
1776:
1772:
1749:(33): 4457–65.
1736:
1735:
1731:
1718:
1717:
1713:
1700:
1699:
1695:
1683:
1674:
1662:
1653:
1649:
1640:
1620:
1555:
1523:
1488:encoded by the
1463:View/Edit Mouse
1458:View/Edit Human
1421:
1414:
1411:Location (UCSC)
1397:
1376:
1350:
1329:
1242:ENSG00000158828
1135:
1116:phosphorylation
1021:TORC2 signaling
734:
618:
599:protein binding
549:kinase activity
509:
499:
498:
471:
462:
457:
455:temporal muscle
453:
449:
445:
441:
437:
433:
429:
425:
423:muscle of thigh
411:
400:
395:
391:
387:
385:muscle of thigh
383:
379:
375:
371:
367:
363:
349:
293:
280:
272:
262:
261:
260:
253:
233:
210:Gene location (
192:
179:
171:
161:
160:
159:
152:
130:
107:Gene location (
58:
45:
38:
17:
12:
11:
5:
3465:
3463:
3455:
3454:
3444:
3443:
3440:
3439:
3432:
3431:External links
3429:
3424:
3423:
3397:(11): 1955–7.
3385:
3342:
3304:(16): 5703–8.
3289:
3259:
3222:
3188:populations".
3184:
3146:
3108:
3056:
3038:(2): 195–201.
3027:
2989:
2951:
2914:
2892:10.1086/319522
2886:(4): 895–900.
2871:
2863:|journal=
2837:
2815:
2813:
2810:
2808:
2807:
2778:(5): 425–429.
2758:
2729:(8): 3518–24.
2709:
2680:(8): 3518–24.
2660:
2611:
2553:
2524:(8): 1308–16.
2504:
2475:(4): 282–295.
2455:
2424:(3): e102537.
2404:
2373:(5): 1638–43.
2353:
2294:
2265:(2): 433–446.
2245:
2196:
2139:
2074:
2031:
2002:(5): 867–869.
1982:
1968:
1939:(6): 864–877.
1917:
1888:(2): 163–172.
1866:
1813:
1770:
1729:
1711:
1693:
1672:
1650:
1648:
1645:
1639:
1636:
1619:
1616:
1554:
1551:
1522:
1519:
1470:
1469:
1466:
1465:
1460:
1450:
1449:
1443:
1442:
1439:
1438:
1436:
1434:
1427:
1426:
1419:
1412:
1408:
1407:
1404:
1403:
1393:
1392:
1386:
1383:
1382:
1372:
1371:
1365:
1361:
1360:
1357:
1356:
1346:
1345:
1339:
1336:
1335:
1325:
1324:
1318:
1314:
1313:
1310:
1309:
1301:
1300:
1294:
1291:
1290:
1282:
1281:
1275:
1269:
1268:
1265:
1264:
1256:
1255:
1249:
1246:
1245:
1237:
1236:
1230:
1224:
1223:
1220:
1219:
1211:
1210:
1204:
1201:
1200:
1192:
1191:
1185:
1179:
1178:
1173:
1168:
1164:
1163:
1153:
1152:
1149:
1148:
1137:
1136:
1134:
1133:
1128:
1123:
1118:
1113:
1108:
1103:
1098:
1093:
1088:
1083:
1078:
1073:
1068:
1063:
1058:
1053:
1048:
1043:
1038:
1033:
1028:
1023:
1018:
1013:
1008:
1003:
998:
993:
988:
983:
978:
973:
968:
963:
958:
953:
948:
943:
938:
933:
928:
923:
918:
913:
908:
903:
898:
893:
888:
883:
878:
873:
868:
863:
858:
853:
848:
843:
838:
833:
828:
823:
818:
813:
808:
803:
798:
796:macroautophagy
793:
788:
783:
778:
773:
768:
763:
758:
753:
748:
742:
740:
736:
735:
733:
732:
727:
722:
717:
712:
707:
702:
697:
692:
687:
682:
677:
672:
667:
662:
657:
652:
647:
642:
637:
632:
626:
624:
620:
619:
617:
616:
611:
606:
601:
596:
591:
586:
581:
576:
571:
566:
561:
556:
551:
546:
540:
538:
534:
533:
523:
522:
519:
518:
515:
514:
506:
505:
487:
481:
480:
477:
476:
468:
467:
464:
463:
461:
460:
456:
452:
448:
444:
440:
436:
432:
428:
424:
420:
417:
416:
405:
402:
401:
399:
398:
394:
390:
386:
382:
378:
374:
370:
366:
362:
358:
355:
354:
342:
341:
333:
322:
316:
315:
312:RNA expression
304:
303:
300:
299:
291:
287:
286:
278:
275:
270:
264:
263:
254:
247:
241:
237:
236:
231:
225:
224:
216:
215:
203:
202:
199:
198:
190:
186:
185:
177:
174:
169:
163:
162:
153:
146:
140:
136:
135:
128:
122:
121:
113:
112:
100:
99:
56:
52:
51:
43:
35:
34:
30:
29:
26:
25:
15:
13:
10:
9:
6:
4:
3:
2:
3464:
3453:
3450:
3449:
3447:
3438:
3435:
3434:
3430:
3428:
3420:
3416:
3412:
3408:
3404:
3400:
3396:
3392:
3386:
3382:
3378:
3374:
3370:
3365:
3360:
3356:
3352:
3348:
3343:
3339:
3335:
3330:
3325:
3320:
3315:
3311:
3307:
3303:
3299:
3295:
3290:
3286:
3282:
3278:
3274:
3270:
3266:
3260:
3256:
3252:
3248:
3244:
3240:
3236:
3233:(8): 1486–8.
3232:
3228:
3223:
3219:
3215:
3211:
3207:
3203:
3199:
3196:(8): 1482–5.
3195:
3191:
3185:
3181:
3177:
3173:
3169:
3165:
3161:
3157:
3153:
3147:
3143:
3139:
3135:
3131:
3127:
3123:
3120:(3): 329–35.
3119:
3115:
3109:
3105:
3101:
3097:
3093:
3088:
3083:
3079:
3075:
3071:
3067:
3063:
3057:
3053:
3049:
3045:
3041:
3037:
3033:
3028:
3024:
3020:
3016:
3012:
3008:
3004:
3000:
2996:
2990:
2986:
2982:
2978:
2974:
2970:
2966:
2962:
2958:
2952:
2948:
2944:
2940:
2936:
2932:
2928:
2925:(6): 849–53.
2924:
2920:
2915:
2911:
2907:
2902:
2897:
2893:
2889:
2885:
2881:
2877:
2872:
2868:
2856:
2848:
2844:
2840:
2834:
2830:
2826:
2822:
2817:
2816:
2811:
2803:
2799:
2794:
2789:
2785:
2781:
2777:
2773:
2769:
2762:
2759:
2754:
2750:
2745:
2740:
2736:
2732:
2728:
2724:
2720:
2713:
2710:
2705:
2701:
2696:
2691:
2687:
2683:
2679:
2675:
2671:
2664:
2661:
2656:
2652:
2647:
2642:
2638:
2634:
2631:(4): 737–47.
2630:
2626:
2622:
2615:
2612:
2607:
2603:
2599:
2595:
2590:
2585:
2581:
2577:
2573:
2569:
2565:
2557:
2554:
2549:
2545:
2540:
2535:
2531:
2527:
2523:
2519:
2515:
2508:
2505:
2500:
2496:
2491:
2486:
2482:
2478:
2474:
2470:
2466:
2459:
2456:
2451:
2447:
2442:
2437:
2432:
2427:
2423:
2419:
2418:PLOS Genetics
2415:
2408:
2405:
2400:
2396:
2391:
2386:
2381:
2376:
2372:
2368:
2364:
2357:
2354:
2349:
2345:
2340:
2335:
2330:
2325:
2321:
2317:
2314:(1): 378–83.
2313:
2309:
2305:
2298:
2295:
2290:
2286:
2281:
2276:
2272:
2268:
2264:
2260:
2256:
2249:
2246:
2241:
2237:
2232:
2227:
2223:
2219:
2215:
2211:
2207:
2200:
2197:
2192:
2188:
2183:
2178:
2174:
2170:
2166:
2162:
2158:
2154:
2150:
2143:
2140:
2135:
2131:
2126:
2121:
2117:
2113:
2109:
2105:
2101:
2097:
2093:
2089:
2085:
2078:
2075:
2070:
2066:
2062:
2058:
2054:
2050:
2047:(3): 266–78.
2046:
2042:
2035:
2032:
2027:
2023:
2018:
2013:
2009:
2005:
2001:
1997:
1993:
1986:
1983:
1978:
1972:
1969:
1964:
1960:
1955:
1950:
1946:
1942:
1938:
1934:
1933:
1928:
1921:
1918:
1913:
1909:
1904:
1899:
1895:
1891:
1887:
1883:
1882:
1877:
1870:
1867:
1862:
1858:
1853:
1848:
1843:
1838:
1834:
1830:
1829:
1824:
1817:
1814:
1809:
1805:
1801:
1797:
1793:
1789:
1786:(3): 336–41.
1785:
1781:
1774:
1771:
1766:
1762:
1757:
1752:
1748:
1744:
1740:
1733:
1730:
1725:
1721:
1715:
1712:
1707:
1703:
1697:
1694:
1690:
1686:
1681:
1679:
1677:
1673:
1669:
1665:
1660:
1658:
1656:
1652:
1646:
1644:
1637:
1635:
1633:
1629:
1625:
1617:
1615:
1613:
1607:
1605:
1599:
1596:
1592:
1584:
1579:
1570:
1566:
1564:
1560:
1552:
1550:
1547:
1544:
1540:
1539:kinase domain
1536:
1532:
1528:
1520:
1518:
1516:
1512:
1508:
1505:
1501:
1500:mitochondrial
1496:
1494:
1491:
1487:
1483:
1479:
1477:
1464:
1459:
1455:
1451:
1448:
1444:
1437:
1435:
1432:
1428:
1424:
1420:
1417:
1413:
1409:
1402:
1400:
1394:
1390:
1387:
1381:
1379:
1373:
1369:
1366:
1362:
1355:
1353:
1347:
1343:
1340:
1334:
1332:
1326:
1322:
1319:
1317:RefSeq (mRNA)
1315:
1308:
1307:
1302:
1298:
1295:
1289:
1288:
1283:
1279:
1276:
1274:
1270:
1263:
1262:
1257:
1253:
1250:
1244:
1243:
1238:
1234:
1231:
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3357:(6): 351–2.
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3158:(3): 424–7.
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1240:
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1195:
1175:
1170:
660:cytoskeleton
335:
328:
294:138,053,618
281:138,040,720
55:External IDs
18:
3152:Ann. Neurol
3114:Ann. Neurol
3032:Cancer Lett
2995:Neurol. Sci
2957:Neurol. Sci
2919:Ann. Neurol
2772:ChemBioChem
1932:J Neurochem
1628:Lewy bodies
730:growth cone
554:ATP binding
273:4|4 D3
193:20,651,511
180:20,633,458
33:Identifiers
1780:Ann Neurol
1691:, May 2017
1670:, May 2017
1647:References
1595:Drosophila
1573:lysosomes.
1543:C-terminal
1535:N-terminal
339:(ortholog)
76:HomoloGene
3391:Neurology
3227:Neurology
3190:Neurology
2865:ignored (
2855:cite book
2116:1476-4687
2041:Autophagy
1632:apoptosis
1612:lysosomes
1563:autophagy
1521:Structure
1511:autophagy
1399:NP_081156
1378:NP_115785
1352:NM_026880
1331:NM_032409
1161:Orthologs
1031:autophagy
720:cell body
685:chromatin
670:Lewy body
630:cytoplasm
84:GeneCards
3446:Category
3419:46024206
3411:15955953
3381:10669009
3373:15876334
3338:15824318
3285:15596610
3255:24418905
3247:15505171
3218:13480500
3210:15505170
3180:10853835
3172:15349870
3134:15349859
3104:33630092
3096:15087508
3052:14607334
3023:21061495
3015:12548371
2985:13625056
2977:12548343
2939:12447943
2910:11254447
2847:17017532
2802:29226533
2753:28323427
2704:28323427
2655:23953109
2606:33630092
2598:15087508
2548:22301916
2499:24446486
2450:22396657
2399:18230723
2348:19966284
2289:18200046
2240:23125018
2191:22936770
2134:29160309
2069:31612944
2061:21187721
2026:21138942
1963:24151868
1912:23319602
1861:20126261
1808:11049051
1800:15349860
1765:11494141
1743:Oncogene
1687:–
1666:–
1553:Function
1541:, and a
1447:Wikidata
1140:Sources:
640:membrane
381:amygdala
3306:Bibcode
3142:1235813
3074:Bibcode
3066:Science
2947:9275470
2901:1275643
2793:5901409
2744:5410652
2695:5410652
2646:3950538
2576:Bibcode
2568:Science
2539:3392634
2490:3989637
2441:3291531
2390:2234197
2339:2806779
2316:Bibcode
2280:2234339
2231:3536340
2182:4762028
2161:Bibcode
2153:Science
2125:6020998
2096:Bibcode
2017:3033179
1954:3951661
1903:3549971
1852:2811155
1689:Ensembl
1668:Ensembl
1507:protein
1273:UniProt
1228:Ensembl
1167:Species
1146:QuickGO
665:nucleus
635:cytosol
393:putamen
314:pattern
172:1p36.12
72:1916193
40:Aliases
3417:
3409:
3379:
3371:
3336:
3329:556294
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2014:
1961:
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1859:
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1806:
1798:
1763:
1504:parkin
1433:search
1431:PubMed
1306:Q99MQ3
1287:Q9BXM7
1183:Entrez
485:BioGPS
365:glutes
64:608309
3415:S2CID
3377:S2CID
3251:S2CID
3214:S2CID
3176:S2CID
3138:S2CID
3100:S2CID
3019:S2CID
2981:S2CID
2943:S2CID
2602:S2CID
2065:S2CID
1804:S2CID
1490:PINK1
1482:PINK1
1216:68943
1197:65018
1176:Mouse
1171:Human
1142:Amigo
447:ankle
337:Mouse
330:Human
277:Start
212:Mouse
176:Start
109:Human
88:PINK1
80:32672
47:PINK1
24:PINK1
3407:PMID
3369:PMID
3334:PMID
3281:PMID
3243:PMID
3206:PMID
3168:PMID
3130:PMID
3092:PMID
3048:PMID
3011:PMID
2973:PMID
2935:PMID
2906:PMID
2867:help
2843:PMID
2833:ISBN
2798:PMID
2749:PMID
2700:PMID
2651:PMID
2625:Cell
2594:PMID
2544:PMID
2495:PMID
2446:PMID
2395:PMID
2344:PMID
2285:PMID
2236:PMID
2187:PMID
2130:PMID
2112:ISSN
2057:PMID
2022:PMID
1959:PMID
1908:PMID
1857:PMID
1796:PMID
1761:PMID
1604:Miro
1583:PARL
1531:PARL
1493:gene
1476:PTEN
715:axon
320:Bgee
268:Band
229:Chr.
167:Band
126:Chr.
60:OMIM
3399:doi
3359:doi
3355:111
3324:PMC
3314:doi
3302:102
3273:doi
3235:doi
3198:doi
3160:doi
3122:doi
3082:doi
3070:304
3040:doi
3036:201
3003:doi
2965:doi
2927:doi
2896:PMC
2888:doi
2825:doi
2788:PMC
2780:doi
2739:PMC
2731:doi
2690:PMC
2682:doi
2641:PMC
2633:doi
2629:154
2584:doi
2572:304
2534:PMC
2526:doi
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2477:doi
2436:PMC
2426:doi
2385:PMC
2375:doi
2371:105
2334:PMC
2324:doi
2312:107
2275:PMC
2267:doi
2226:PMC
2218:doi
2177:PMC
2169:doi
2157:337
2120:PMC
2104:doi
2092:552
2049:doi
2012:PMC
2004:doi
1949:PMC
1941:doi
1937:128
1898:PMC
1890:doi
1886:200
1847:PMC
1837:doi
1788:doi
1751:doi
290:End
189:End
92:OMA
68:MGI
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