Epsin family proteins bind ubiquitinated cargo

Stable Identifier
R-HSA-8866279
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
9723620 Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis

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

Nature 1998
19696798 Endocytosis and signalling: intertwining molecular networks

von Zastrow, M, Sorkin, A

Nat. Rev. Mol. Cell Biol. 2009
24384571 Ubiquitin-dependent sorting in endocytosis

Lukacs, GL, Piper, RC, Dikic, I

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

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

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

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

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

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

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

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

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

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

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

Drubin, DG, Weinberg, JS

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

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

Biomol Concepts 2012
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!