QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online July 12, 2005

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?

Endocytic motif defies consensus...

Proteins internalized at the cell surface by clathrin-mediated endocytosis contain specific sorting sequences that bind to the internalization machinery. The best characterized of these is the tyrosine-based YXX motif (in which X is any residue and is a bulky, hydrophobic residue). This binds to a specific region in the µ2 subunit of the AP2 clathrin adaptor protein, and structural studies have shown that the spacing between the Y and residues is crucial. Ruth Murrell and co-workers now unveil a novel type of tyrosine-based endocytic motif (p. 3073). They have used site-directed mutagenesis and CD8-based chimeras to analyse endocytosis of P2X4 receptors, ATP-gated cation channels that rapidly cycle off the plasma membrane. These receptors possess consensus YXX motifs, but surprisingly these are inaccessible to AP2 and not needed for endocytosis. Instead, the authors show, a downstream YXXG motif is required. Determining the structure of a YXXG–µ2 complex, they demonstrate that the motif recognizes the same region of µ2 but accommodates the extra G residue by altering its backbone configuration. These findings thus define a second type of AP2-binding tyrosine motif, extending the range of sequences that could drive internalization.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

Related articles in JCS:

Non-canonical YXXG endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors

Stephen J. Royle, Omar S. Qureshi, Laura K. Bobanovic, Philip R. Evans, David J. Owen, and Ruth D. Murrell-Lagnado
JCS 2005 118: 3073-3080. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?