Epsin 1 is a polyubiquitin-selective clathrin-associated sorting protein - PubMed

Epsin 1 is a polyubiquitin-selective clathrin-associated sorting protein

Matthew J Hawryluk et al. Traffic. 2006 Mar.

Free article

Erratum in

• Traffic. 2006 Jul;7(7):927

Abstract

Epsin 1 engages several core components of the endocytic clathrin coat, yet the precise mode of operation of the protein remains controversial. The occurrence of tandem ubiquitin-interacting motifs (UIMs) suggests that epsin could recognize a ubiquitin internalization tag, but the association of epsin with clathrin-coat components or monoubiquitin is reported to be mutually exclusive. Here, we show that endogenous epsin 1 is clearly an integral component of clathrin coats forming at the cell surface and is essentially absent from caveolin-1-containing structures under normal conditions. The UIM region of epsin 1 associates directly with polyubiquitin chains but has extremely poor affinity for monoubiquitin. Polyubiquitin binding is retained when epsin synchronously associates with phosphoinositides, the AP-2 adaptor complex and clathrin. The enrichment of epsin within clathrin-coated vesicles purified from different tissue sources varies and correlates with sorting of multiubiquitinated cargo, and in cultured cells, polyubiquitin, rather than non-conjugable monoubiquitin, promotes rapid internalization. As epsin interacts with eps15, which also contains a UIM region that binds to polyubiquitin, epsin and eps15 appear to be central components of the vertebrate poly/multiubiquitin-sorting endocytic clathrin machinery.

Comment in

• Ubiquitin binding in endocytosis--how tight should it be and where does it happen?

  Madshus IH. Madshus IH. Traffic. 2006 Mar;7(3):258-61. doi: 10.1111/j.1600-0854.2006.00393.x. Traffic. 2006. PMID: 16497221

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