Willox, Anna K. and Royle, Stephen J. (2012) Functional analysis of interaction sites on the n-terminal domain of clathrin heavy chain. Traffic, 13 (1). pp. 70-81. doi:10.1111/j.1600-0854.2011.01289.x

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Abstract

In clathrin-mediated membrane traffic, clathrin does not bind directly to cargo and instead binds to adaptors that mediate this function. For endocytosis, the main adaptor is the adaptor protein (AP)-2 complex, but it is uncertain how clathrin contacts AP-2. Here we tested in human cells the importance of the three binding sites that have been identified so far on the N-terminal domain (NTD) of clathrin. We find that mutation of each of the three sites on the NTD, alone or in combination, does not block clathrin/AP-2-mediated endocytosis in the same way as deletion of the NTD. We report here the fourth and final site on the NTD that is required for clathrin/AP-2-mediated endocytic function. Each of the four interaction sites can operate alone to mediate endocytosis. The observed functional redundancy between interaction sites on the NTD explains how productivity of clathrin-coated vesicle formation is ensured.

Item Type:	Journal Article
Divisions:	Faculty of Medicine > Warwick Medical School
Journal or Publication Title:	Traffic
Publisher:	Wiley-Blackwell Publishing Ltd.
ISSN:	1398-9219
Official Date:	January 2012
Dates:	Date Event January 2012 Published
Volume:	13
Number:	1
Page Range:	pp. 70-81
DOI:	10.1111/j.1600-0854.2011.01289.x
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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