Talk:Epsin

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Contents

[edit] Removed section

The following section may be correct, but the content looks unreadable even for the most of biologists. I actually do not know how to simplify it properly. Maybe it would be better to get without it:

[edit] Epsin1

Epsin 1 is a brain enriched 94 kDa protein that interacts with ubiquitin via its UIM domains, it interacts with the EH domains of Eps15 and Eps15R via its 3 NPF motifs, it interacts with the alpha appendage domains of AP2 adaptors via DPW motifs and it interacts with clathrin via its clathrin terminal domain binding motifs. This same domain has motifs for clathrin interactions. Given the PtdIns(4,5)P2 specificity of epsin1 and epsin2 they are assumed to be plasma membrane adaptors.

[edit] Epsin3

Epsin 3 is almost exclusively localised to migrating keratinocytes in cutaneous wounds.

[edit] EpsinR

Epsin 4/EpsinR/enthoprotin/Clint is thought to be involved in the budding of clathrin-coated vesicles from intracellular compartments. It binds to AP1 adaptors rather than AP2.

pubmed

  • Kay BK, Yamabhai M, Wendland B, Emr SD. (1999) Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8, 435-8. pubmed
  • Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. (2001) Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 291, 1047-51. pubmed
  • Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. (2002) Curvature of clathrin-coated pits driven by epsin. Nature 419, 361-6. pubmed
  • Stahelin RV, Long F, Peter BJ, Murray D, De Camilli P, McMahon HT, Cho W.(2003) Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. Aug 278, 28993-9. pubmed


Audriusa 17:17, 8 April 2007 (UTC)