17:
141:, and co-regulating certain cell cycle control proteins. Much of hnRNPs' importance to cell cycle control is evidenced by its role as an oncogene, in which a loss of its functions results in various common cancers. Often, misregulation by hnRNPs is due to splicing errors, but some hnRNPs are also responsible for recruiting and guiding the proteins themselves, rather than just addressing nascent RNAs.
225:). p53 suppression of genes is often carried out by a number of these lincRNAs, which in turn have been shown to act though hnRNP K. Through physical interactions with these molecules, hnRNP K is targeted to genes and transmits p53 regulation, thus acting as a key repressor within the p53-dependent transcriptional pathway.
129:. hnRNPs are also responsible for strengthening and inhibiting splice sites by making such sites more or less accessible to the spliceosome. Cooperative interactions between attached hnRNPs may encourage certain splicing combinations while inhibiting others.
164:
progression of the cell is impaired. Additionally, BRCA1 and BRCA2 levels fall when hnRNP C is lost. BRCA1 and BRCA2 are crucial tumor-suppressor genes which are strongly implicated in breast cancers when mutated. BRCA1 in particular causes
247:
The association of a pre-mRNA molecule with a hnRNP particle prevents formation of short secondary structures dependent on base pairing of complementary regions, thereby making the pre-mRNA accessible for interactions with other proteins.
173:
signaling cascade. hnRNP C is important for the proper expression of other tumor suppressor genes including RAD51 and BRIP1 as well. Through these genes, hnRNP is necessary to induce cell-cycle arrest in response to DNA damage by
189:
is overexpressed in 20-30% of breast cancers and is commonly associated with poor prognosis. It is therefore an oncogene whose differently spliced variants have been shown to have different functions. Knocking down
50:
of the newly synthesized RNA (pre-mRNA). The presence of the proteins bound to a pre-mRNA molecule serves as a signal that the pre-mRNA is not yet fully processed and therefore not ready for export to the
299:, the protein responsible for elongating telomeres and prevent their degradation. hnRNPs C1 and C2 associate with the RNA component of telomerase, which improves its ability to access the telomere.
86:
shows nucleoplasmic localization of these proteins with little staining in the nucleolus or cytoplasm. This is likely because of its major role in binding to newly transcribed RNAs. High-resolution
214:
is rapidly induced after DNA damage by ionizing radiation. It cooperates with p53 to induce the activation of p53 target genes, thus activating cell-cycle checkpoints. p53 itself is an important
547:
Beyer, Ann L.; Christensen, Mark E.; Walker, Barbara W.; LeStourgeon, Wallace M. (1977). "Identification and characterization of the packaging proteins of core 40S hnRNP particles".
194:
was shown to increase the amount of an oncogenic variant Δ16HER2. HER2 is an upstream regulator of cyclin D1 and p27, and its overexpression leads to the deregulation of the
264:, through splicing mechanisms. CD44 is involved in cell-cell interactions and has roles in cell adhesion and migration. Splicing of CD44 and the functions of the resulting
1782:
1772:
1767:
1747:
1727:
1392:
Ford, Lance P.; Wright, Woodring E.; Shay, Jerry W. (2002-01-21). "A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation".
1123:
Huarte, Maite; Guttman, Mitchell; Feldser, David; Garber, Manuel; Koziol, Magdalena J.; Kenzelmann-Broz, Daniela; Khalil, Ahmad M.; Zuk, Or; Amit, Ido (2010).
1698:
1229:
Loh, Tiing Jen; Moon, Heegyum; Cho, Sunghee; Jang, Hana; Liu, Yong Chao; Tai, Hongmei; Jung, Da-Woon; Williams, Darren R.; Kim, Hey-Ran (September 2015).
218:
sometimes known by the epithet “the guardian of the genome.” hnRNP K’s close association with p53 demonstrates its importance in DNA damage control.
67:
1666:
796:
699:
590:
Dreyfuss, Gideon; Matunis, Michael J.; Pinol-Roma, Serafin; Burd, Christopher G. (1993-06-01). "hnRNP Proteins and the
Biogenesis of mRNA".
388:
102:
828:
Anantha, Rachel W.; Alcivar, Allen L.; Ma, Jianglin; Cai, Hong; Simhadri, Srilatha; Ule, Jernej; König, Julian; Xia, Bing (2013-04-09).
1757:
1752:
78:(NLS) and are therefore found mainly in the nucleus. Though it is known that a few hnRNPs shuttle between the cytoplasm and nucleus,
59:
in the nucleus exist as heterogeneous ribonucleoprotein particles. After splicing has occurred, the proteins remain bound to spliced
1495:
715:
Matlin, Arianne J.; Clark, Francis; Smith, Christopher W. J. (2005). "Understanding alternative splicing: towards a cellular code".
47:
1691:
769:
Martinez-Contreras, Rebeca; Cloutier, Philippe; Shkreta, Lulzim; Fisette, Jean-François; Revil, Timothée; Chabot, Benoit (2007).
1174:"The role of interactions of long non-coding RNAs and heterogeneous nuclear ribonucleoproteins in regulating cellular functions"
960:
Gautrey, Hannah; Jackson, Claire; Dittrich, Anna-Lena; Browell, David; Lennard, Thomas; Tyson-Capper, Alison (2015-10-03).
75:
1927:
1901:
1684:
289:
98:
97:
The proteins involved in the hnRNP complexes are collectively known as heterogeneous ribonucleoproteins. They include
160:
genes. In response to ionizing radiation, hnRNP C partially localizes to the site of DNA damage, and when depleted,
1485:
237:
Preventing the folding of pre-mRNA into secondary structures that may inhibit its interactions with other proteins.
166:
635:"Ultrastructural distribution of nuclear ribonucleoproteins as visualized by immunocytochemistry on thin sections"
221:
p53 regulates a large group of RNAs that are not translated into protein, called large intergenic noncoding RNAs (
268:
are different in breast cancer cells, and when knocked down, hnRNP reduced both cell viability and invasiveness.
830:"Requirement of Heterogeneous Nuclear Ribonucleoprotein C for BRCA Gene Expression and Homologous Recombination"
1922:
43:
1614:"Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro"
897:"Role of BRCA1 and BRCA2 as regulators of DNA repair, transcription, and cell cycle in response to DNA damage"
413:
74:
and therefore important for the translation of mRNA in the cytoplasm. However, hnRNPs also have their own
1337:"Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase"
215:
1437:"The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins"
1280:"In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance"
1231:"CD44 alternative splicing and hnRNP A1 expression are associated with the metastasis of breast cancer"
1019:"The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis"
1529:
1125:"A Large Intergenic Noncoding RNA Induced by p53 Mediates Global Gene Repression in the p53 Response"
841:
493:
138:
126:
1885:
1793:
1707:
222:
87:
56:
1518:"Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein"
1105:
942:
748:
572:
175:
79:
288:
associates with the G-rich repeat region of the telomeres, possibly stabilizing the region from
690:
Matsudaira PT, Lodish HF, Berk A, Kaiser C, Krieger M, Scott MP, Bretscher A, Ploegh H (2008).
323:
319:
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1201:
1185:
1144:
1136:
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989:
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867:
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784:
724:
662:
646:
599:
556:
519:
501:
408:
403:
364:
110:
1676:
1076:"hnRNP K: An HDM2 Target and Transcriptional Coactivator of p53 in Response to DNA Damage"
265:
195:
106:
1533:
929:
896:
845:
603:
497:
16:
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524:
481:
1916:
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1279:
1074:
Moumen, Abdeladim; Masterson, Philip; O'Connor, Mark J.; Jackson, Stephen P. (2005).
560:
459:
1109:
946:
752:
576:
261:
114:
39:
977:
1172:
Sun, Xinghui; Ali, Mohamed Sham
Shihabudeen Haider; Moran, Matthew (2017-09-01).
854:
788:
122:
1140:
1092:
1075:
962:"SRSF3 and hnRNP H1 regulate a splicing hotspot of HER2 in breast cancer cells"
1849:
1586:
296:
281:
55:. Since most mature RNA is exported from the nucleus relatively quickly, most
1462:
1413:
1360:
1303:
1256:
1197:
1042:
985:
920:
863:
806:
736:
658:
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515:
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91:
52:
1604:
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1405:
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1321:
1264:
1215:
1158:
1101:
1060:
1034:
1003:
938:
881:
814:
744:
506:
482:"Detection of mRNA sequences in nuclear 30S ribonucleoprotein subcomplexes"
1649:
1470:
676:
619:
533:
1865:
1247:
1230:
779:. Advances in Experimental Medicine and Biology. Vol. 623. pp.
650:
568:
331:
315:
277:
186:
83:
71:
1189:
233:
hnRNP serves a variety of processes in the cell, some of which include:
1818:
1800:
1789:
424:
336:
311:
307:
Human genes encoding heterogeneous nuclear ribonucleoproteins include:
161:
35:
1640:
90:
has shown that hnRNPs localize predominantly to the border regions of
1833:
1828:
1823:
1762:
1742:
1732:
1335:
Ford, L. P.; Suh, J. M.; Wright, W. E.; Shay, J. W. (December 2000).
419:
399:
394:
383:
379:
375:
359:
355:
346:
327:
191:
149:
60:
728:
206:
hnRNPs also play a role in DNA damage response in coordination with
1661:. San Francisco: Pearson/Benjamin Cummings. pp. ch. 9 and 10.
1777:
1737:
1719:
1571:"The hnRNP Family: Insights into Their Role in Health and Disease"
430:
285:
211:
170:
157:
153:
15:
284:
from deterioration and are often associated with cell longevity.
447:
369:
257:
207:
118:
1680:
137:
hnRNPs affect several aspects of the cell cycle by recruiting,
1612:
Takimoto M, Tomonaga T, Matunis M, et al. (August 1993).
31:
1516:
Xie J, Lee JA, Kress TL, Mowry KL, Black DL (July 2003).
462:: complex between mRNA and protein(s) present in nucleus
1484:
Dityatev, Alexander; El-Husseini, Alaa (2006-11-24).
1435:
Görlach, M.; Burd, C. G.; Dreyfuss, G. (1994-09-16).
633:
Fakan, S.; Leser, G.; Martin, T. E. (January 1984).
169:
cell cycle arrest in response to DNA damage via the
1894:
1874:
1858:
1842:
1809:
1718:
895:Yoshida, Kiyotsugu; Miki, Yoshio (November 2004).
770:
1569:Geuens T, Delphine B, Timmerman V (August 2016).
240:Possible association with the splicing apparatus.
486:Proceedings of the National Academy of Sciences
480:Kinniburgh, A. J.; Martin, T. E. (1976-08-01).
1692:
94:, where it has access to these nascent RNAs.
8:
777:Alternative Splicing in the Postgenomic Era
295:hnRNP has also been shown to interact with
1699:
1685:
1677:
292:which would inhibit telomere replication.
1639:
1629:
1594:
1551:
1541:
1452:
1368:
1311:
1278:Eversole, A.; Maizels, N. (August 2000).
1246:
1205:
1148:
1091:
1050:
993:
928:
871:
853:
666:
523:
505:
24:Heterogeneous nuclear ribonucleoproteins
472:
1487:Molecular Mechanisms of Synaptogenesis
772:"HNRNP Proteins and Splicing Control"
717:Nature Reviews Molecular Cell Biology
243:Transport of mRNA out of the nucleus.
7:
764:
762:
103:polypyrimidine tract-binding protein
1441:The Journal of Biological Chemistry
604:10.1146/annurev.bi.62.070193.001445
113:and is responsible for suppressing
913:10.1111/j.1349-7006.2004.tb02195.x
14:
256:hnRNP has been shown to regulate
133:Role in cell cycle and DNA damage
63:and target them for degradation.
48:post-transcriptional modification
1353:10.1128/mcb.20.23.9084-9091.2000
1296:10.1128/mcb.20.15.5425-5432.2000
66:hnRNPs are also integral to the
694:. San Francisco: W.H. Freeman.
1341:Molecular and Cellular Biology
1284:Molecular and Cellular Biology
76:nuclear localization sequences
1:
1659:Molecular biology of the gene
1631:10.1016/S0021-9258(17)46837-2
1454:10.1016/S0021-9258(17)31621-6
978:10.1080/15476286.2015.1076610
592:Annual Review of Biochemistry
276:Several hnRNPs interact with
105:(PTB), which is regulated by
80:immunofluorescence microscopy
1522:Proc. Natl. Acad. Sci. U.S.A
855:10.1371/journal.pone.0061368
561:10.1016/0092-8674(77)90323-3
280:, which protect the ends of
1902:Signal recognition particle
789:10.1007/978-0-387-77374-2_8
639:The Journal of Cell Biology
1944:
1141:10.1016/j.cell.2010.06.040
1093:10.1016/j.cell.2005.09.032
152:is a key regulator of the
121:by blocking access of the
1657:Watson, James D. (2004).
1587:10.1007/s00439-016-1683-5
88:immunoelectron microscopy
1876:Vault ribonucleoprotein
1543:10.1073/pnas.1432696100
1406:10.1038/sj.onc.1205086
1035:10.1038/sj.onc.1210477
692:Molecular cell biology
507:10.1073/pnas.73.8.2725
20:
1017:Moasser, M M (2007).
216:tumor-suppressor gene
19:
1248:10.3892/or.2015.4110
651:10.1083/jcb.98.1.358
290:secondary structures
127:polypyrimidine tract
82:with hnRNP-specific
1886:Major vault protein
1843:Other transcription
1794:U1 spliceosomal RNA
1708:RNA-binding protein
1534:2003PNAS..100.8776X
1447:(37): 23074–23078.
1190:10.1042/bcj20170280
1178:Biochemical Journal
846:2013PLoSO...861368A
498:1976PNAS...73.2725K
57:RNA-binding protein
30:) are complexes of
1928:Ribonucleoproteins
1712:Ribonucleoproteins
176:ionizing radiation
44:gene transcription
21:
1910:
1909:
1668:978-0-8053-4635-0
1347:(23): 9084–9091.
1290:(15): 5425–5432.
1184:(17): 2925–2935.
1029:(45): 6469–6487.
972:(10): 1139–1151.
798:978-0-387-77373-5
701:978-0-7167-7601-7
260:, a cell-surface
1935:
1701:
1694:
1687:
1678:
1672:
1653:
1643:
1633:
1624:(24): 18249–58.
1608:
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1502:
1501:
1481:
1475:
1474:
1456:
1432:
1426:
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1372:
1332:
1326:
1325:
1315:
1275:
1269:
1268:
1250:
1241:(3): 1231–1238.
1235:Oncology Reports
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1220:
1219:
1209:
1169:
1163:
1162:
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1120:
1114:
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1095:
1086:(6): 1065–1078.
1071:
1065:
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1007:
997:
957:
951:
950:
932:
892:
886:
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624:
623:
587:
581:
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527:
509:
492:(8): 2725–2729.
477:
117:at a particular
111:protein kinase A
1943:
1942:
1938:
1937:
1936:
1934:
1933:
1932:
1923:Gene expression
1913:
1912:
1911:
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1854:
1838:
1805:
1714:
1705:
1675:
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1611:
1568:
1528:(15): 8776–81.
1515:
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1509:Further reading
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907:(11): 866–871.
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729:10.1038/nrm1645
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305:
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252:CD44 Regulation
231:
204:
184:
147:
135:
107:phosphorylation
70:subunit of the
46:and subsequent
38:present in the
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1575:Human Genetics
1566:
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1496:
1476:
1427:
1400:(4): 580–583.
1384:
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1135:(3): 409–419.
1115:
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901:Cancer Science
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758:
723:(5): 386–398.
707:
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645:(1): 358–363.
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598:(1): 289–321.
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555:(1): 127–138.
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1618:J. Biol. Chem
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1581:(8): 851–67.
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262:glycoprotein
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198:checkpoint.
185:
148:
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115:RNA splicing
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65:
40:cell nucleus
27:
23:
22:
1859:Translation
966:RNA Biology
282:chromosomes
123:spliceosome
1917:Categories
1850:Telomerase
1641:2115/72478
467:References
297:telomerase
84:antibodies
1878:particles
1463:0021-9258
1414:0950-9232
1361:0270-7306
1304:0270-7306
1257:1791-2431
1198:0264-6021
1043:1476-5594
986:1547-6286
921:1347-9032
864:1932-6203
807:0065-2598
737:1471-0080
659:0021-9525
612:0066-4154
516:0027-8424
427:(SYNCRIP)
416:(FUS/TLS)
332:HNRNPA2B1
324:HNRNPA1L2
320:HNRNPA1L1
278:telomeres
272:Telomeres
229:Functions
99:protein K
92:chromatin
53:cytoplasm
1866:Ribosome
1801:SNRNP200
1605:27215579
1562:12851456
1422:11850782
1394:Oncogene
1379:11074006
1322:10891483
1265:26151392
1216:28801479
1159:20673990
1110:16756766
1102:16360036
1061:17471238
1023:Oncogene
1004:26367347
947:24297965
939:15546503
930:11159131
882:23585894
834:PLOS ONE
815:18380344
753:14883495
745:15956978
577:41245800
454:See also
443:HNRNPUL3
439:HNRNPUL2
435:HNRNPUL1
358:(AUF1),
351:HNRNPCL1
303:Examples
266:isoforms
223:lincRNAs
192:hnRNP H1
139:splicing
72:ribosome
1650:8349701
1596:4947485
1530:Bibcode
1471:8083209
1207:5553131
1150:2956184
1052:3021475
995:4829299
873:3621867
842:Bibcode
781:123–147
677:6231300
668:2113018
620:8352591
534:1066686
494:Bibcode
414:HNRNPP2
384:HNRNPH3
380:HNRNPH2
376:HNRNPH1
342:HNRNPB1
337:HNRNPAB
328:HNRNPA3
316:HNRNPA1
312:HNRNPA0
286:hnRNP D
212:hnRNP K
162:S-phase
150:hnRNP C
125:to the
61:introns
42:during
36:protein
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569:872217
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431:HNRNPU
425:HNRNPQ
420:HNRNPR
409:HNRNPM
404:HNRPLL
400:HNRNPL
395:HNRNPK
389:HNRNPI
372:(RBMX)
370:HNRNPG
365:HNRNPF
360:HNRPDL
356:HNRNPD
347:HNRNPC
28:hnRNPs
1895:Other
1811:hnRNP
1720:snRNP
1370:86561
1313:85994
1106:S2CID
943:S2CID
749:S2CID
573:S2CID
391:(PTB)
171:CHEK1
158:BRCA2
154:BRCA1
145:BRCA1
1663:ISBN
1646:PMID
1601:PMID
1558:PMID
1492:ISBN
1467:PMID
1459:ISSN
1418:PMID
1410:ISSN
1375:PMID
1357:ISSN
1318:PMID
1300:ISSN
1261:PMID
1253:ISSN
1212:PMID
1194:ISSN
1155:PMID
1129:Cell
1098:PMID
1080:Cell
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1000:PMID
982:ISSN
935:PMID
917:ISSN
878:PMID
860:ISSN
811:PMID
803:ISSN
793:ISBN
741:PMID
733:ISSN
696:ISBN
673:PMID
655:ISSN
616:PMID
608:ISSN
565:PMID
549:Cell
530:PMID
512:ISSN
448:FMR1
258:CD44
196:G1/S
187:HER2
182:HER2
167:G2/M
156:and
119:exon
101:and
34:and
1790:70K
1636:hdl
1626:doi
1622:268
1591:PMC
1583:doi
1579:135
1548:PMC
1538:doi
1526:100
1449:doi
1445:269
1402:doi
1365:PMC
1349:doi
1308:PMC
1292:doi
1243:doi
1202:PMC
1186:doi
1182:474
1145:PMC
1137:doi
1133:142
1088:doi
1084:123
1047:PMC
1031:doi
990:PMC
974:doi
925:PMC
909:doi
868:PMC
850:doi
785:doi
725:doi
663:PMC
647:doi
600:doi
557:doi
520:PMC
502:doi
208:p53
202:p53
68:40S
32:RNA
1919::
1819:A0
1763:D3
1758:D2
1753:D1
1743:B2
1733:A1
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1834:R
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Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
