Epsin family proteins bind ubiquitinated cargo

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R-HSA-8866279
Type
Reaction
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Homo sapiens
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Summation

Some membrane cargo is sorted into clathrin-coated pits after ubiquitination of the cytosolic domain (reviewed in Piper et al 2014). Ubiquitinated cargo is recognized by adaptor proteins such as EPS15, EPN1 and EPN2 that contain ubiquitin-binding domains and also interact with components of the clathrin coat (Chen et al, 1998; Rosenthal et al, 1999; Polo et al, 2002; Shih et al, 2002; Haglund et al, 2003; Schmid et al, 2006; reviewed in Sen et al, 2012; Piper et al, 2014). A number of receptor tyrosine kinases, including EGFR, VEGFR, FGFR and others undergo ubiquitination at the plasma membrane, triggering endocytosis. Internalized RTKs can undergo recycling or degradation, the latter of which serves to terminate signaling (reviewed in Sorkin and von Zastrow, 2009; Haglund and Dikic, 2012). Ubiquitin-based sorting into CCPs appears to be dynamic as deubiquitinases have been identified as components of some CCPs (Weinberg and Drubin, 2014).

Literature References
PubMed ID Title Journal Year
19696798 Endocytosis and signalling: intertwining molecular networks

Sorkin, A, von Zastrow, M

Nat. Rev. Mol. Cell Biol. 2009
9723620 Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis

Chen, H, Fre, S, Slepnev, VI, Capua, MR, Takei, K, Butler, MH, Di Fiore, PP, De Camilli, P

Nature 1998
24384571 Ubiquitin-dependent sorting in endocytosis

Piper, RC, Dikic, I, Lukacs, GL

Cold Spring Harb Perspect Biol 2014
16903783 Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly

Schmid, EM, Ford, MG, Burtey, A, Praefcke, GJ, Peak-Chew, SY, Mills, IG, Benmerah, A, McMahon, HT

PLoS Biol. 2006
11988742 Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis

Shih, SC, Katzmann, DJ, Schnell, JD, Sutanto, M, Emr, SD, Hicke, L

Nat. Cell Biol. 2002
22357968 The role of ubiquitylation in receptor endocytosis and endosomal sorting

Haglund, K, Dikic, I

J. Cell. Sci. 2012
12717448 Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation

Haglund, K, Sigismund, S, Polo, S, Szymkiewicz, I, Di Fiore, PP, Dikic, I

Nat. Cell Biol. 2003
11919637 A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins

Polo, S, Sigismund, S, Faretta, M, Guidi, M, Capua, MR, Bossi, G, Chen, H, De Camilli, P, Di Fiore, PP

Nature 2002
10567358 The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module

Rosenthal, JA, Chen, H, Slepnev, VI, Pellegrini, L, Salcini, AE, Di Fiore, PP, De Camilli, P

J Biol Chem 1999
24746795 Regulation of clathrin-mediated endocytosis by dynamic ubiquitination and deubiquitination

Weinberg, JS, Drubin, DG

Curr. Biol. 2014
22942912 The epsin protein family: coordinators of endocytosis and signaling

Sen, A, Madhivanan, K, Mukherjee, D, Aguilar, RC

Biomol Concepts 2012
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