445:
537:-like protein that associates with microtubules. Cep55 then recruits the Vps23 subunit of ESCRT-I and accessory protein ALIX, which form into rings on either side of the midbody. ESCRT-I and ALIX recruit ESCRT-III via its Snf7 subunit. ESCRT-III subunits Vps20, Snf7, Vps24, Vps2, and Did2 form into a spiral-shaped fibril adjacent to the rings formed by Vps23. The formation of this spiral-like structure deforms the membrane and the AAA-ATPase spastin is brought in by Did2 and Ist1 to cleave the microtubules formed at the midbody. Vps4 then
359:, then Vps2) for the machinery to function. Nonessential subunits include Vps60, Did2, and Ist1. Vps20 initiates assembly of ESCRT-III by acting as a nucleator of Snf7 polymer assembly. Vps24 then associates with Snf7 to cap the complex and recruit Vps2. Vps2 then brings Vps4 to the complex. All “free” cytosolic forms of each subunit are considered closed. That is, the carboxy-terminal portion of each subunit folds up onto itself in an autoinhibitory manner stabilizing the
499:
1911:
333:(WH) motifs of Vps22 and Vps36 creating a Y-shaped complex with Vps22 and Vps36 as the base and Vps25 molecules as arms. Vps25 molecules also contain WH motifs that are responsible for the interaction of ESCRT-II with ESCRT-III. Vps36 contains a GLUE domain that binds phosphatidylinositol 3-phosphate and Vps28 of ESCRT-I. Two
551:
394:
The Vps4-Vta1 proteins are required for the stripping of other ESCRT components (usually ESCRT-III) from membranes once a particular process has been completed. There is some debate as to whether Vps4 cleaves the ESCRT-III complex away or remodels the complex so one component is shed at a particular
345:
The ESCRT-III complex is likely the most important of all the ESCRT machinery because it plays a role in all ESCRT mediated processes. During membrane abscission and viral budding, ESCRT-III forms long filaments that coil around the site of membrane constriction just prior to membrane cleavage. This
313:
The ESCRT-II complex functions primarily during the biogenesis of multivesicular bodies and delivery of ubiquitin tagged proteins to the endosome. Ubiquitin tagged proteins are passed from ESCRT-0 to ESCRT-I and then to ESCRT-II. ESCRT-II associates with ESCRT-III, which pinches the cargo containing
594:
of the ESCRT-I complex and the ALIX accessory protein. ESCRT-III subunits (only CHMP4 and CHMP2 being essential) are recruited to the site of viral budding to constrict and sever the neck of the bud in a manner similar to that described for membrane abscission during cytokinesis. Vps4 then recycles
428:
to the ESCRT-III complex. This results in the removal of ubiquitin tags from proteins targeted for degradation in the lysosome just prior to the generation of multivesicular bodies. It has also been speculated that Bro1 helps stabilize ESCRT-III while ubiquitin tags are cleaved from cargo proteins.
557:
A) Accumulation of viral proteins under the cell membrane causes the virus to protrude outward. B) A constriction is formed by the ESCRT complexes at the base of membrane protrusion causing formation of a virus containing vesicle. C) The bud pinches off leaving a free extracellular virion. (Photo
227:
The role of the ESCRT-I complex is to assist in the generation of multivesicular bodies by clustering ubiquitinated proteins and acting as a bridge between the ESCRT-0 and ESCRT-II complexes. It also plays a role in membrane recognition and remodeling during membrane abscission by forming rings on
459:
play a large role in the transport of ubiquitinated proteins and receptors to a lysosome. ESCRT complexes transport ubiquitinated cargo to cellular vesicles that bud directly into the cell’s endosomal compartment, forming multivesicular bodies. These multivesicular bodies eventually fuse with the
398:
Vps4 subunits have two functional domains, an amino-terminal MIT domain and a central AAA-ATPase domain. The MIT domain is responsible for the interaction of Vps4 with the MIM domain of Vps2. The AAA-ATPase domain hydrolyzes ATP to power disassembly of the ESCRT-III complex. This “stripping” of
232:
of dividing cells. ESCRT-I is also responsible for recruiting ESCRT-III, which forms the constriction zone just before the cells separate. Furthermore, ESCRT-I plays a role in viral budding by interacting with specific viral proteins, leading to recruitment of additional ESCRT machinery to the
122:
451:
Membrane bound proteins are taken into the cell via endocytosis. Ubiquitin tags on the protein are recognized by ESCRT machinery and recruited to the endosome. Multivesicular bodies are formed, which then fuse with the lysosome where these proteins are degraded. Adapted
350:
complex. These filamentous structures are also present during multivesicular body formation and function as a ring-like fence that plugs the budding vesicle to prevent cargo proteins from escaping into the cell's cytosol. ESCRT-III exists and functions as follows:
105:(HSP). Cellular abscission, the process by which the membrane connecting two daughter cells is cleaved, is also mediated by ESCRT machinery. Without the ESCRT complexes, daughter cells could not separate and abnormal cells containing twice the amount of
415:
IP5), which enables binding to Vps4, and a MIT domain for associating with ESCRT-III subunit Vps60. Though not essential, Vta1 has been shown to aid in Vps4 ring assembly, accelerate the ATPase activity of Vsp4, and encourage ESCRT-III disassembly.
541:
the disassembly of the ESCRT-III complex resulting in two newly separated daughter cells. The process of membrane abscission was described using metazoan proteins as the process has been studied to a greater extent in metazoans.
354:
The ESCRT-III complex differs from all other ESCRT machinery in that it exists only transiently and contains both essential and nonessential components. The essential subunits must assemble in the proper order (Vps20, Snf7,
210:
TAM proteins). These VHS domains bind the ubiquitin on proteins the cell aims to degrade. Ubiquitin can also associate with ubiquitin interacting motifs such as the one on Hse1 or the double sided domain found on Vps27. A
129:
Each of the ESCRT complexes and accessory proteins have unique structures that enable distinct biochemical functions. A number of synonyms exist for each protein component of the ESCRT machinery, both for yeast and
113:. Lastly, viral budding, or the process by which specific types of viruses exit cells, may not occur in the absence of ESCRT machinery. This would inevitably prevent viruses from spreading from cell to cell.
595:
the ESCRT-III components to the cytosol and the virus is released from the cell. The mechanism described here utilizes metazoan proteins, as viral budding has been studied more extensively in metazoans.
505:
Cep-55 binds MKLP1. Cep-55 recruits ESCRT-I and ALIX. ESCRT-I and ALIX recruit ESCRT-III. ESCRT-III forms spiral around membrane neck between daughter cells leading to constriction and cleavage. Adapted
215:(named after the four proteins in which it was initially identified: Fab1p, YOTB, Vac1, and EEA1) is found sandwiched between the VHS and ubiquitin interacting motif domains of Vps27.
337:
domains are looped into the GLUE domain of yeast Vps36. One of these zinc finger domains binds the carboxy-terminal domain of Vps28 and the other associates with ubiquitin.
395:
time. Vta1 is thought to act as an activator of Vps4, aiding its assembly and enhancing its AAA-ATPase activity. The manner in which these proteins function is as follows:
436:
domain of Doa4, an ubiquitin hydrolase (deubiquitinase), bringing it to the site of abscission. Doa4 removes ubiquitin from cargo proteins being targeted to the lysosome.
590:, require ESCRT machinery to exit the host cell. The process is initiated by viral Gag proteins, the major structural proteins of retroviral coats, which interact with
248:
of Vps23, Vps28, and Vps37. Vps23 contains one ubiquitin E2 variant domain, which is responsible for the binding of ubiquitin, the ESCRT-0 complex, and to the PTAP (
42:
protein complexes, known as ESCRT-0, ESCRT-I, ESCRT-II, and ESCRT-III. Together with a number of accessory proteins, these ESCRT complexes enable a unique mode of
432:
Bro1 contains a Bro1 amino-terminal domain that binds to Snf7 of ESCRT-III. This binding brings Bro1 to the site of membrane abscission. Bro1 also binds the
244:, Vps37, and Mvb12. The assembled heterotetramer appears as a rod-shaped stalk composed of Vps23, Vps37, and Mvb12 with a fanned cap composed of single
161:
where they are degraded. This process is essential as it is the major pathway for the degradation of damaged proteins that have passed through the
97:. This process is essential for cells to destroy misfolded and damaged proteins. Without ESCRT machinery, these proteins can build up and lead to
1856:"Recruitment of MKLP1 to the spindle midzone/midbody by INCENP is essential for midbody formation and completion of cytokinesis in human cells"
839:
489:
rings upon which Vta1 binds. This Vps4-Vta1 complex triggers the disassembly of ESCRT-III and marks the end of multivesicular body formation.
460:
lysosome causing degradation of the cargo. A more in-depth description of the process, including associated machinery, exists as follows:
145:
The ESCRT-0 complex plays a vital role in the generation of multivesicular bodies by binding and clustering ubiquitinated proteins and/or
1111:"Comparative genomics reveals selective distribution and domain organization of FYVE and PX domain proteins across eukaryotic lineages"
157:, these proteins are then taken into the endosome via vesicles, forming multivesicular bodies, and are eventually delivered to the
216:
94:
467:
Vps27 binds to phosphatidylinositol 3-phosphate, an endosomal lipid, which then recruits the entire complex to an endosome.
102:
822:
Samson, RY; Dobro, MJ; Jensen, GJ; Bell, SD (2017). "The
Structure, Function and Roles of the Archaeal ESCRT Apparatus".
470:
Vps27 binds the Vps23 subunit of ESCRT-I, bringing ESCRT-I to the endosome. ESCRT-I can also bind ubiquitinated proteins.
55:
1480:"ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation"
185:
281:
Y) is present that directs ESCRT-I to the midbody during membrane abscission. Mvb12 can also bind ubiquitin via its
1901:
579:
17:
219:, a common endosomal lipid, binds to this FYVE domain resulting in the recruitment of ESCRT-0 to the endosome.
173:
154:
444:
525:, membrane abscission is considered to be the earliest role for ESCRT machinery. The process begins when the
425:
146:
363:
subunits. The carboxy-terminus of most ESCRT-III subunits, both essential and nonessential, contain MIMs (
274:
229:
1931:
285:. Vps28 is responsible for the interaction of ESCRT-I and ESCRT-II by associating with the GLUE domain (
558:
provided by Dr. Matthew Gonda (Wikimedia
Commons: Nov. 1998), National Cancer Institute Image ID: 2382)
498:
101:
disease. For example, abnormalities in ESCRT-III components can lead to neurological disorders such as
1540:
1450:
1016:
1936:
473:
Vps36 associates with ESCRT-I subunit Vps28, resulting in the recruitment of the ESCRT-II complex.
195:
153:
on the endosomal membrane, which recruits these tagged proteins to the endosome. Once properly
1885:
1836:
1787:
1727:
1675:
1617:
1568:
1527:
Scott A, Gaspar J, Stuchell-Brereton MD, Alam SL, Skalicky JJ, Sundquist WI (September 2005).
1509:
1432:
1376:
1322:
1258:
1194:
1142:
1091:
1042:
985:
897:
845:
835:
804:
732:
680:
181:
98:
1773:
883:
403:
is a dimeric protein containing one VSL domain (so named because it is found in the proteins
1875:
1867:
1826:
1818:
1777:
1769:
1717:
1709:
1665:
1657:
1607:
1599:
1558:
1548:
1499:
1491:
1422:
1414:
1366:
1358:
1312:
1304:
1248:
1240:
1184:
1176:
1163:
Morita E, Sandrin V, McCullough J, Katsuyama A, Baci
Hamilton I, Sundquist WI (March 2011).
1132:
1122:
1081:
1073:
1032:
1024:
975:
967:
887:
879:
827:
794:
786:
722:
714:
670:
662:
538:
433:
330:
1588:"Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1"
121:
50:. These ESCRT components have been isolated and studied in a number of organisms including
1455:
347:
162:
109:
would be generated. These cells would inevitably be destroyed through a process known as
1544:
1020:
233:
potential site of viral release. Details of the ESCRT-I machinery are described below.
1915:
1880:
1855:
1831:
1806:
1782:
1757:
1722:
1697:
1670:
1645:
1612:
1587:
1563:
1528:
1504:
1479:
1427:
1402:
1371:
1346:
1317:
1292:
1253:
1228:
1189:
1164:
1137:
1110:
1086:
1061:
1037:
1004:
980:
955:
892:
867:
799:
774:
727:
702:
675:
650:
583:
237:
1586:
Azmi I, Davies B, Dimaano C, Payne J, Eckert D, Babst M, Katzmann DJ (February 2006).
1925:
1661:
1398:
1062:"VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo"
703:"MVB vesicle formation: ESCRT-dependent, ESCRT-independent and everything in between"
518:
517:
is the process by which the membrane connecting two daughter cells is cleaved during
78:
43:
380:
302:
191:
GAT (so named after proteins GGA and Tom1) domains. Both Vps27 and Hse1 contain an
69:
The ESCRT machinery plays a vital role in a number of cellular processes including
1244:
971:
831:
1758:"The ESCRT complexes: structure and mechanism of a membrane-trafficking network"
587:
514:
476:
Vps25 subunit of ESCRT-II binds to and activates Vps20 of the ESCRT-III complex.
368:
334:
245:
212:
188:
169:
1910:
1529:"Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A"
1180:
570:
are released from within cells via the hijacking of host cell ESCRT machinery.
1698:"Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast"
1308:
718:
666:
571:
526:
282:
192:
74:
59:
449:
Trafficking of membrane bound proteins to the lysosome using ESCRT machinery.
1553:
1127:
775:"Membrane budding and scission by the ESCRT machinery: it's all in the neck"
479:
Vps20 nucleates the formation of Snf7 strands that are then capped by Vps24.
360:
256:
110:
86:
82:
47:
1889:
1840:
1791:
1731:
1696:
Wemmer M, Azmi I, West M, Davies B, Katzmann D, Odorizzi G (January 2011).
1679:
1621:
1572:
1513:
1495:
1436:
1380:
1347:"No strings attached: the ESCRT machinery in viral budding and cytokinesis"
1326:
1262:
1198:
1146:
1095:
1046:
989:
901:
849:
808:
736:
684:
533:
is recruited to the midbody of dividing cells in association with MKLP1, a
149:
on the surface of a cell. The complex is then responsible for binding to a
1713:
1603:
1005:"Molecular mechanism of multivesicular body biogenesis by ESCRT complexes"
277:. Just after this ubiquitin E2 variant domain, a proline rich motif (GPPX
1077:
399:
ESCRT-III allows all associated subunits to be recycled for further use.
158:
90:
70:
1822:
1028:
1871:
1362:
534:
522:
486:
383:
263:
249:
137:
In yeast, the following complexes/accessory proteins exist as follows:
63:
39:
1229:"Assembly and disassembly of the ESCRT-III membrane scission complex"
591:
131:
1418:
790:
379:
otif) motifs. These motifs are responsible for binding Vps4 and the
464:
ESCRT-0 components Vps27 and Hse1 each bind to ubiquitinated cargo.
46:
remodeling that results in membranes bending/budding away from the
1807:"Abscission checkpoint control: stuck in the middle with Aurora B"
1403:"Dynamics of ESCRT protein recruitment during retroviral assembly"
567:
549:
530:
497:
443:
356:
326:
322:
318:
241:
150:
51:
314:
vesicle closed. The specific aspects of ESCRT-II are as follows:
550:
400:
177:
1451:"Cytokinesis: Centralspindlin Moonlights as a Membrane Anchor"
575:
134:. A summary table of all of these proteins is provided below.
106:
346:
mediation of abscission occurs through interactions with the
81:. Multivesicular body (MVB) biogenesis is a process in which
826:. Subcellular Biochemistry. Vol. 84. pp. 357–377.
329:
subunit. Vps25 molecules contain PPXY motifs, which bind to
165:. The components of the ESCRT-0 complex exist as follows:
1646:"Regulation of Vps4 during MVB sorting and cytokinesis"
1293:"Membrane abscission: first glimpse at dynamic ESCRTs"
482:
Vps24 recruits Vps2, which brings Vps4 to the complex.
1899:
317:
ESCRT-II is a heterotetramer (2:1:1) composed of two
1478:Teis D, Saksena S, Judson BL, Emr SD (March 2010).
1165:"ESCRT-III protein requirements for HIV-1 budding"
868:"Biogenesis and function of multivesicular bodies"
440:Multivesicular body biogenesis and cargo shuttling
125:Summary of ESCRT machinery and accessory proteins.
32:endosomal sorting complexes required for transport
18:Endosomal sorting complexes required for transport
1644:Babst M, Davies BA, Katzmann DJ (October 2011).
562:The release of viral particles, also known as
503:Recruitment of ESCRT Complexes to the Midbody.
8:
1854:Zhu C, Bossy-Wetzel E, Jiang W (July 2005).
1751:
1749:
1747:
1745:
1743:
1741:
301:AP45) of Vps36 through its carboxy-terminal
1392:
1390:
1340:
1338:
1336:
1291:Mueller M, Adell MA, Teis D (August 2012).
1345:McDonald B, Martin-Serrano J (July 2009).
1286:
1284:
1282:
1280:
1278:
1276:
1274:
1272:
768:
766:
644:
642:
640:
638:
636:
634:
632:
630:
628:
1879:
1830:
1781:
1721:
1691:
1689:
1669:
1639:
1637:
1635:
1633:
1631:
1611:
1562:
1552:
1503:
1426:
1370:
1316:
1252:
1188:
1158:
1156:
1136:
1126:
1085:
1036:
979:
949:
947:
945:
943:
941:
939:
937:
935:
933:
931:
891:
798:
764:
762:
760:
758:
756:
754:
752:
750:
748:
746:
726:
674:
626:
624:
622:
620:
618:
616:
614:
612:
610:
608:
1774:10.1146/annurev.biophys.35.040405.102126
1222:
1220:
1218:
1216:
1214:
1212:
1210:
1208:
929:
927:
925:
923:
921:
919:
917:
915:
913:
911:
884:10.1146/annurev.cellbio.23.090506.123319
424:The main function of Bro1 is to recruit
120:
1906:
1473:
1471:
1469:
1467:
1465:
861:
859:
696:
694:
604:
521:. Since it is conserved in a number of
117:ESCRT complexes and accessory proteins
1109:Banerjee S, Basu S, Sarkar S (2010).
198:(so named because it is contained in
7:
773:Hurley JH, Hanson PI (August 2010).
1003:Wollert T, Hurley JH (April 2010).
649:Schmidt O, Teis D (February 2012).
371:interacting and transport domain)
25:
1227:Adell MA, Teis D (October 2011).
27:Protein complexes in cell biology
1909:
1662:10.1111/j.1600-0854.2011.01230.x
217:Phosphatidylinositol 3-phosphate
58:, the machinery is found in all
1060:Ren X, Hurley JH (March 2010).
1762:Annu Rev Biophys Biomol Struct
866:Piper RC, Katzmann DJ (2007).
485:Vps4 forms a pore made of two
1:
1245:10.1016/j.febslet.2011.09.001
960:Crit. Rev. Biochem. Mol. Biol
566:, is a process by which free
103:hereditary spastic paraplegia
1533:Proc. Natl. Acad. Sci. U.S.A
972:10.3109/10409238.2010.502516
832:10.1007/978-3-319-53047-5_12
56:eukaryotic signature protein
954:Hurley JH (December 2010).
73:(MVB) biogenesis, cellular
1953:
1756:Hurley JH, Emr SD (2006).
1181:10.1016/j.chom.2011.02.004
580:human T-lymphotropic virus
555:Retroviral budding of HIV.
38:) machinery is made up of
1401:, Simon SM (April 2011).
1309:10.1016/j.cub.2012.06.063
872:Annu. Rev. Cell Dev. Biol
824:Prokaryotic Cytoskeletons
719:10.1016/j.ceb.2011.04.008
667:10.1016/j.cub.2012.01.028
582:, as well as a number of
236:The ESCRT-I complex is a
779:Nat. Rev. Mol. Cell Biol
174:vacuolar protein sorting
1805:Carmena M (July 2012).
1554:10.1073/pnas.0502165102
1397:Jouvenet N, Zhadina M,
1128:10.1186/1471-2164-11-83
701:Babst M (August 2011).
273:roline) motif of viral
85:-tagged proteins enter
1496:10.1038/emboj.2009.408
559:
507:
453:
126:
1714:10.1083/jcb.201007018
1604:10.1083/jcb.200508166
956:"The ESCRT complexes"
707:Curr. Opin. Cell Biol
651:"The ESCRT machinery"
553:
501:
457:Multivesicular bodies
447:
168:The complex is a 1:1
124:
93:via the formation of
1078:10.1038/emboj.2010.6
297:biquitin-binding in
240:(1:1:1:1) of Vps23,
228:either side of the
1823:10.1098/rsob.120095
1545:2005PNAS..10213813S
1029:10.1038/nature08849
1021:2010Natur.464..864W
511:Membrane abscission
494:Membrane abscission
71:multivesicular body
1872:10.1042/BJ20050097
1459:, 18 February 2013
1449:Glotzer, Michael.
1363:10.1242/jcs.028308
1357:(Pt 13): 2167–77.
560:
508:
454:
127:
1169:Cell Host Microbe
841:978-3-319-53045-1
584:enveloped viruses
303:four-helix bundle
180:. Vps27 and Hse1
99:neurodegenerative
16:(Redirected from
1944:
1914:
1913:
1905:
1894:
1893:
1883:
1866:(Pt 2): 373–81.
1851:
1845:
1844:
1834:
1802:
1796:
1795:
1785:
1753:
1736:
1735:
1725:
1693:
1684:
1683:
1673:
1656:(10): 1298–305.
1641:
1626:
1625:
1615:
1583:
1577:
1576:
1566:
1556:
1524:
1518:
1517:
1507:
1475:
1460:
1447:
1441:
1440:
1430:
1394:
1385:
1384:
1374:
1342:
1331:
1330:
1320:
1288:
1267:
1266:
1256:
1224:
1203:
1202:
1192:
1160:
1151:
1150:
1140:
1130:
1106:
1100:
1099:
1089:
1057:
1051:
1050:
1040:
1000:
994:
993:
983:
951:
906:
905:
895:
863:
854:
853:
819:
813:
812:
802:
770:
741:
740:
730:
698:
689:
688:
678:
646:
586:, including the
283:carboxy-terminus
176:protein 27) and
21:
1952:
1951:
1947:
1946:
1945:
1943:
1942:
1941:
1922:
1921:
1920:
1908:
1900:
1898:
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1853:
1852:
1848:
1804:
1803:
1799:
1755:
1754:
1739:
1695:
1694:
1687:
1643:
1642:
1629:
1585:
1584:
1580:
1539:(39): 13813–8.
1526:
1525:
1521:
1477:
1476:
1463:
1456:Current Biology
1448:
1444:
1419:10.1038/ncb2207
1396:
1395:
1388:
1344:
1343:
1334:
1290:
1289:
1270:
1226:
1225:
1206:
1162:
1161:
1154:
1108:
1107:
1103:
1059:
1058:
1054:
1015:(7290): 864–9.
1002:
1001:
997:
953:
952:
909:
865:
864:
857:
842:
821:
820:
816:
791:10.1038/nrm2937
772:
771:
744:
700:
699:
692:
648:
647:
606:
601:
548:
535:mitotic kinesin
496:
442:
426:deubiquitinases
422:
392:
348:centralspindlin
343:
311:
280:
225:
143:
119:
28:
23:
22:
15:
12:
11:
5:
1950:
1948:
1940:
1939:
1934:
1924:
1923:
1919:
1918:
1896:
1895:
1846:
1797:
1737:
1708:(2): 295–306.
1685:
1627:
1578:
1519:
1461:
1442:
1413:(4): 394–401.
1407:Nat. Cell Biol
1386:
1332:
1303:(15): R603–5.
1268:
1239:(20): 3191–6.
1204:
1152:
1101:
1072:(6): 1045–54.
1052:
995:
907:
855:
840:
814:
742:
690:
661:(4): R116–20.
603:
602:
600:
597:
547:
544:
495:
492:
491:
490:
483:
480:
477:
474:
471:
468:
465:
441:
438:
421:
418:
391:
388:
342:
339:
321:subunits, one
310:
307:
278:
238:heterotetramer
224:
221:
193:amino-terminal
142:
139:
118:
115:
54:and humans. A
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1949:
1938:
1935:
1933:
1930:
1929:
1927:
1917:
1912:
1907:
1903:
1891:
1887:
1882:
1877:
1873:
1869:
1865:
1861:
1857:
1850:
1847:
1842:
1838:
1833:
1828:
1824:
1820:
1817:(7): 120095.
1816:
1812:
1808:
1801:
1798:
1793:
1789:
1784:
1779:
1775:
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1686:
1681:
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1667:
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1659:
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1647:
1640:
1638:
1636:
1634:
1632:
1628:
1623:
1619:
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1609:
1605:
1601:
1598:(5): 705–17.
1597:
1593:
1589:
1582:
1579:
1574:
1570:
1565:
1560:
1555:
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1546:
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1538:
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1520:
1515:
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1506:
1501:
1497:
1493:
1490:(5): 871–83.
1489:
1485:
1481:
1474:
1472:
1470:
1468:
1466:
1462:
1458:
1457:
1452:
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1234:
1230:
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1217:
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1209:
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1200:
1196:
1191:
1186:
1182:
1178:
1175:(3): 235–42.
1174:
1170:
1166:
1159:
1157:
1153:
1148:
1144:
1139:
1134:
1129:
1124:
1120:
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1079:
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1018:
1014:
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999:
996:
991:
987:
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977:
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969:
966:(6): 463–87.
965:
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957:
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815:
810:
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801:
796:
792:
788:
785:(8): 556–66.
784:
780:
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769:
767:
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763:
761:
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724:
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695:
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664:
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613:
611:
609:
605:
598:
596:
593:
589:
585:
581:
577:
573:
569:
565:
564:viral budding
556:
552:
546:Viral budding
545:
543:
540:
536:
532:
528:
524:
520:
519:cell division
516:
512:
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135:
133:
123:
116:
114:
112:
108:
104:
100:
96:
92:
88:
84:
80:
79:viral budding
76:
72:
67:
65:
61:
57:
53:
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45:
41:
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33:
19:
1932:Cell anatomy
1863:
1859:
1849:
1814:
1810:
1800:
1765:
1761:
1705:
1702:J. Cell Biol
1701:
1653:
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1592:J. Cell Biol
1591:
1581:
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1410:
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1350:
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1115:BMC Genomics
1114:
1104:
1069:
1065:
1055:
1012:
1008:
998:
963:
959:
875:
871:
823:
817:
782:
778:
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710:
706:
658:
654:
572:Retroviruses
563:
561:
554:
510:
509:
502:
456:
455:
448:
431:
423:
412:
408:
404:
397:
393:
376:
372:
364:
353:
344:
331:winged-helix
316:
312:
298:
294:
290:
286:
275:Gag proteins
270:
264:
257:
250:
235:
226:
207:
203:
199:
186:antiparallel
167:
144:
136:
128:
68:
35:
31:
29:
1399:Bieniasz PD
1351:J. Cell Sci
588:Ebola virus
527:centrosomal
515:cytokinesis
375:nteracting
369:microtubule
335:zinc finger
213:FYVE domain
189:coiled-coil
170:heterodimer
1937:Organelles
1926:Categories
1860:Biochem. J
1768:: 277–98.
1297:Curr. Biol
878:: 519–47.
655:Curr. Biol
599:References
574:, such as
381:AAA-ATPase
325:, and one
196:VHS domain
172:of Vps27 (
87:organelles
75:abscission
60:eukaryotes
1811:Open Biol
1233:FEBS Lett
539:catalyzes
487:hexameric
434:catalytic
411:BP1, and
390:Vps4-Vta1
361:monomeric
341:ESCRT-III
155:localized
147:receptors
132:metazoans
111:apoptosis
91:endosomes
83:ubiquitin
62:and some
48:cytoplasm
40:cytosolic
1890:15796717
1841:22870391
1792:16689637
1732:21263029
1680:21658171
1622:16505166
1573:16174732
1514:20134403
1437:21394083
1381:19535732
1327:22877781
1263:21924267
1199:21396898
1147:20122178
1096:20150893
1047:20305637
990:20653365
902:17506697
850:28500532
809:20588296
737:21570275
685:22361144
529:protein
309:ESCRT-II
305:domain.
260:hreonine
206:RS, and
184:through
182:dimerize
159:lysosome
95:vesicles
44:membrane
1916:Biology
1881:1175114
1832:3411112
1783:1648078
1723:3172170
1671:3171586
1650:Traffic
1613:2063703
1564:1236530
1541:Bibcode
1505:2837172
1428:3245320
1372:2723143
1318:3414845
1254:3192940
1190:3070458
1138:2837644
1087:2845278
1038:2851844
1017:Bibcode
981:2988974
893:2911632
800:2922035
728:3148405
676:3314914
568:virions
523:archaea
513:during
384:spastin
246:helices
230:midbody
223:ESCRT-I
141:ESCRT-0
89:called
64:archaea
1902:Portal
1888:
1878:
1839:
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1790:
1780:
1730:
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1484:EMBO J
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1066:EMBO J
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1009:Nature
988:
978:
900:
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735:
725:
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592:TSG101
267:lanine
253:roline
202:ps27,
77:, and
576:HIV-1
531:Cep55
506:from.
452:from.
407:ps4,
357:Vps24
327:Vps36
323:Vps22
319:Vps25
242:Vps28
163:Golgi
151:lipid
52:yeast
36:ESCRT
1886:PMID
1837:PMID
1788:PMID
1728:PMID
1676:PMID
1618:PMID
1569:PMID
1510:PMID
1433:PMID
1377:PMID
1323:PMID
1259:PMID
1195:PMID
1143:PMID
1092:PMID
1043:PMID
986:PMID
898:PMID
846:PMID
836:ISBN
805:PMID
733:PMID
681:PMID
578:and
420:Bro1
401:Vta1
367:IT (
293:ike
289:RAM-
178:Hse1
30:The
1876:PMC
1868:doi
1864:389
1827:PMC
1819:doi
1778:PMC
1770:doi
1718:PMC
1710:doi
1706:192
1666:PMC
1658:doi
1608:PMC
1600:doi
1596:172
1559:PMC
1549:doi
1537:102
1500:PMC
1492:doi
1423:PMC
1415:doi
1367:PMC
1359:doi
1355:122
1313:PMC
1305:doi
1249:PMC
1241:doi
1237:585
1185:PMC
1177:doi
1133:PMC
1123:doi
1082:PMC
1074:doi
1033:PMC
1025:doi
1013:464
976:PMC
968:doi
888:PMC
880:doi
828:doi
795:PMC
787:doi
723:PMC
715:doi
671:PMC
663:doi
107:DNA
1928::
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