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Table 1.

Interactions between and requirement for ESCRT subunits in MVB biogenesis, viral-particle release and cytokinesis in mammalian cells715

Role in:
Subunit* Known interaction partners MVB biogenesis Viral budding Cytokinesis
ESCRT-0     
   HRS   Tsg101, STAM, PtdIns(3)P, ubiquitin, SNAP25, VPS37A, clathrin, Cep55   Required for EGFR and EGF degradation1,2  Not required3  Recruited to midbody4 
   STAM1 and STAM2   HRS, UBPY, ubiquitin, AMSH   Required for EGFR degradation5  N.D.   N.D.  
ESCRT-I     
   Tsg101 (Vps23)   All ESCRT-I subunits, EAP30, EAP45, ALIX, HRS, Bcr, TOM1, TOM1L1, TOM1L2, ubiquitin, Cep55, Rock1, IQGAP, CD2AP, HD-PTP   Recruited by HRS to endosomal membrane; required for EGFR and EGF degradation2,6-9  Recruited to plasma membrane by HIV-1 Gag to mediate virus budding10,11  Recruited to midbody by Cep55 to mediate abscission12,13 
   VPS28-I and VPS28-II   Tsg101, CHMP6, Bcr, ESCRT-II   Blocking antibody inhibits EGF degradation8  Required14-16  Required12 
   VPS37A, B, C, D   Tsg101, Cep55; VPS37A binds to HRS   VPS37A required for EGFR degradation17  VPS37B and VPS37C required for HIV-1 release16,18  N.D.  
   MVB12A, MVB12B   Tsg101; MVB12A binds to VPS37B   Recruited to aberrant endosomes19  Role in maturation and/or infectivity of HIV-119  N.D.  
ESCRT-II     
   EAP30, EAP20, EAP45   CHMP6, VPS28-I, ubiquitin, Tsg101, with one another   May be required for EGFR degradation; not required for MHC-1 degradation20,21  Not required20  N.D.  
ESCRT-III     
   CHMP1A and CHMP1B (Did2) – contain MIM   MITD1, UBPY, LIP5, AMSH, hIST1, VPS4, with one another; CHIMP1B binds to CHMP2A, CHMP4B, CHMP5, spastin   GFP fusion causes aberrant endosomes22  Overexpressed YFP fusion inhibits budding23  Required for abscission24 
   CHMP2A and CHMP2B (Vps2) – contain MIM   CHMP2A binds to AMSH, MITD1, VPS4, CHMP1B, CHMP3, CHMP4A, CHMP4B, CHMP5; CHMP2B binds to CHMP3   Expression of truncated form causes aberrant endosomes25  CHMP2A-YFP fusion inhibits budding; CHMP2B has no DN effect26,27  CHMP2A recruited to midbody13 
   CHMP3 (Vps24)   CHMP2A, CHMP2B, CHMP4B, VPS4, AMSH   Required for proper EGFR degradation28  Overexpressed YFP fusion inhibits budding26  Abscission inhibited by DN mutant29 
   CHMP4A, B, C (Snf7) – contain MIM2   CHMP6, ALIX, Brox, HD-PTP, VPS4, with one another; CHMP4B binds to CHMP1B, CHMP3, CHMP5, CHMP7; CHMP4C binds to AMSH, UBPY   Expression of a truncated form causes aberrant endosomes25  YFP fusion proteins inhibit budding26,27,30  Required for abscission30,13 
   CHMP5 (Vps60)   CHMP1B, CHMP2A, CHMP4A, CHMP4B, LIP5   Required for proper EGFR and TGFβR degradation31,32  YFP fusion was shown to inhibit, but depletion enhanced, virus release27,31  Recruited to midbody13 
   CHMP6 (Vps20) – contains MIM2   CHMP4A, CHMP4B, EAP45, EAP20, EAP30, VPS28-I, VPS4   Required for proper EGFR degradation20  Not required20  N.D.  
   CHMP7   CHMP4B   GFP fusion inhibits EGFR degradation33  GFP fusion inhibits VLP release33  N.D.  
ESCRT-associated proteins     
   ALIX   Tsg101, endophilin, CHMP4A, CHMP4B, CHMP4C, Cep55, CD2AP, Cin85   Not essential for EGFR degradation34,35  Required for EIAV budding; minor activity in HIV-1 release36,27  Recruited by Cep55 to midbody to mediate abscission12,13 
ESCRT-associated proteins      
   LIP5 – contains MIT domains   CHMP1A, CHMP1B, CHMP5, VPS4, hIST1   Required for proper EGFR degradation31  Required for HIV-1 release31  Binding partners are required24,40 
   VPS4A, VPS4B – contain MIT domain   CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C, LIP5, hIST1   Required for dissociation of complexes from endosomal membrane37  Required for viral budding11,26  Abscission inhibited by DN mutant13 
   AMSH – contains MIT domain   CHMP1A, CHMP1B, CHMP2A, CHMP3, CHMP4C, STAM, hIST1   Depletion increases rate of EGFR degradation38  Not essential23  Recruited to midbody; depletion causes moderate defect4 
   UBPY – contains MIT domain   CHMP1A, CHMP1B, CHMP4C, STAM, hIST1   Required for deubiquitylation of EGFR39  N.D.   Catalytic mutant inhibits abscission; recruited to midbody4 
   hIST – contains MIM1 and MIM2   CHMP1A, CHMP1B, MITD1, spastin, VPS4, LIP5, AMSH, UBPY   Not required for EGFR degradation40  Not essential24,40  Required for abscission24,26 
Role in:
Subunit* Known interaction partners MVB biogenesis Viral budding Cytokinesis
ESCRT-0     
   HRS   Tsg101, STAM, PtdIns(3)P, ubiquitin, SNAP25, VPS37A, clathrin, Cep55   Required for EGFR and EGF degradation1,2  Not required3  Recruited to midbody4 
   STAM1 and STAM2   HRS, UBPY, ubiquitin, AMSH   Required for EGFR degradation5  N.D.   N.D.  
ESCRT-I     
   Tsg101 (Vps23)   All ESCRT-I subunits, EAP30, EAP45, ALIX, HRS, Bcr, TOM1, TOM1L1, TOM1L2, ubiquitin, Cep55, Rock1, IQGAP, CD2AP, HD-PTP   Recruited by HRS to endosomal membrane; required for EGFR and EGF degradation2,6-9  Recruited to plasma membrane by HIV-1 Gag to mediate virus budding10,11  Recruited to midbody by Cep55 to mediate abscission12,13 
   VPS28-I and VPS28-II   Tsg101, CHMP6, Bcr, ESCRT-II   Blocking antibody inhibits EGF degradation8  Required14-16  Required12 
   VPS37A, B, C, D   Tsg101, Cep55; VPS37A binds to HRS   VPS37A required for EGFR degradation17  VPS37B and VPS37C required for HIV-1 release16,18  N.D.  
   MVB12A, MVB12B   Tsg101; MVB12A binds to VPS37B   Recruited to aberrant endosomes19  Role in maturation and/or infectivity of HIV-119  N.D.  
ESCRT-II     
   EAP30, EAP20, EAP45   CHMP6, VPS28-I, ubiquitin, Tsg101, with one another   May be required for EGFR degradation; not required for MHC-1 degradation20,21  Not required20  N.D.  
ESCRT-III     
   CHMP1A and CHMP1B (Did2) – contain MIM   MITD1, UBPY, LIP5, AMSH, hIST1, VPS4, with one another; CHIMP1B binds to CHMP2A, CHMP4B, CHMP5, spastin   GFP fusion causes aberrant endosomes22  Overexpressed YFP fusion inhibits budding23  Required for abscission24 
   CHMP2A and CHMP2B (Vps2) – contain MIM   CHMP2A binds to AMSH, MITD1, VPS4, CHMP1B, CHMP3, CHMP4A, CHMP4B, CHMP5; CHMP2B binds to CHMP3   Expression of truncated form causes aberrant endosomes25  CHMP2A-YFP fusion inhibits budding; CHMP2B has no DN effect26,27  CHMP2A recruited to midbody13 
   CHMP3 (Vps24)   CHMP2A, CHMP2B, CHMP4B, VPS4, AMSH   Required for proper EGFR degradation28  Overexpressed YFP fusion inhibits budding26  Abscission inhibited by DN mutant29 
   CHMP4A, B, C (Snf7) – contain MIM2   CHMP6, ALIX, Brox, HD-PTP, VPS4, with one another; CHMP4B binds to CHMP1B, CHMP3, CHMP5, CHMP7; CHMP4C binds to AMSH, UBPY   Expression of a truncated form causes aberrant endosomes25  YFP fusion proteins inhibit budding26,27,30  Required for abscission30,13 
   CHMP5 (Vps60)   CHMP1B, CHMP2A, CHMP4A, CHMP4B, LIP5   Required for proper EGFR and TGFβR degradation31,32  YFP fusion was shown to inhibit, but depletion enhanced, virus release27,31  Recruited to midbody13 
   CHMP6 (Vps20) – contains MIM2   CHMP4A, CHMP4B, EAP45, EAP20, EAP30, VPS28-I, VPS4   Required for proper EGFR degradation20  Not required20  N.D.  
   CHMP7   CHMP4B   GFP fusion inhibits EGFR degradation33  GFP fusion inhibits VLP release33  N.D.  
ESCRT-associated proteins     
   ALIX   Tsg101, endophilin, CHMP4A, CHMP4B, CHMP4C, Cep55, CD2AP, Cin85   Not essential for EGFR degradation34,35  Required for EIAV budding; minor activity in HIV-1 release36,27  Recruited by Cep55 to midbody to mediate abscission12,13 
ESCRT-associated proteins      
   LIP5 – contains MIT domains   CHMP1A, CHMP1B, CHMP5, VPS4, hIST1   Required for proper EGFR degradation31  Required for HIV-1 release31  Binding partners are required24,40 
   VPS4A, VPS4B – contain MIT domain   CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C, LIP5, hIST1   Required for dissociation of complexes from endosomal membrane37  Required for viral budding11,26  Abscission inhibited by DN mutant13 
   AMSH – contains MIT domain   CHMP1A, CHMP1B, CHMP2A, CHMP3, CHMP4C, STAM, hIST1   Depletion increases rate of EGFR degradation38  Not essential23  Recruited to midbody; depletion causes moderate defect4 
   UBPY – contains MIT domain   CHMP1A, CHMP1B, CHMP4C, STAM, hIST1   Required for deubiquitylation of EGFR39  N.D.   Catalytic mutant inhibits abscission; recruited to midbody4 
   hIST – contains MIM1 and MIM2   CHMP1A, CHMP1B, MITD1, spastin, VPS4, LIP5, AMSH, UBPY   Not required for EGFR degradation40  Not essential24,40  Required for abscission24,26 

Abbreviations not included in main text: DN, dominant-negative; EGFR, epidermal growth factor receptor; EIAV, equine infectious anaemia virus; GFP, green fluorescent protein; N.D. not determined; PtdIns(3)P, phosphatidylinositol 3-phosphate; TGFβR, transforming growth factor-β receptor; VLP, virus-like particle; YFP, yellow fluorescent protein

*

Yeast nomenclature is shown in parentheses

1

(Urbe et al., 2003)

2

(Raiborg et al., 2008)

3

(Pornillos et al., 2003)

4

(Mukai et al., 2008)

5

(Kanazawa et al., 2003)

6

(Bache et al., 2003)

7

(Katzmann et al., 2003)

8

(Bishop et al., 2002)

9

(Babst et al., 2000)

10

(Martin-Serrano et al., 2001)

11

(Garrus et al., 2001)

12

(Carlton and Martin-Serrano, 2007)

13

(Morita et al., 2007b)

14

(Martin-Serrano et al., 2003a)

15

(Tanzi et al., 2003)

16

(Stuchell et al., 2004)

17

(Bache et al., 2004)

18

(Eastman et al., 2005)

19

(Morita et al., 2007a)

20

(Langelier et al., 2006)

21

(Bowers et al., 2006)

22

(Howard et al., 2001)

23

(Agromayor and Martin-Serrano, 2006)

24

(Bajorek et al., 2009)

25

(Shim et al., 2007)

26

(von Schwedler et al., 2003)

27

(Martin-Serrano et al., 2003b)

28

(Bache et al., 2006)

29

(Dukes et al., 2008)

30

(Carlton et al., 2008)

31

(Ward et al., 2005)

32

(Shim et al., 2006)

33

(Horii et al., 2006)

34

(Schmidt et al., 2004)

35

(Cabezas et al., 2005)

36

(Strack et al., 2003)

37

(Babst et al., 1998)

38

(McCullough et al., 2004)

39

(Row et al., 2007)

40

(Agromayor et al., 2009)

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