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First published online September 22, 2005

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UBL traffic signals for aggresomes

Eps15 is an essential component in the clathrin-mediated endocytic pathway. In common with several other components of this pathway, Eps15 contains ubiquitin-interacting motifs (UIMs). However, the role of these UIMs in the regulation of intracellular transport is not clear. Paul van Bergen en Henegouwen and colleagues now report that Eps15 and some other UIM-containing endocytic proteins are recruited through their UIMs into ubiquitin-rich cytoplasmic aggregates by ubiquilin, a ubiquitin-like protein (see p. 4437). The authors initially detected the Eps15-ubiquilin interaction in a 2-hybrid assay and then used GST pulldown experiments to show that the first UIM of Eps15 interacts directly with the ubiquitin-like (UBL) domain of ubiquilin. Other experiments indicate that the endocytic proteins Hrs and Hbp (but not epsin) also interact with ubiquilin in a UIM-dependent manner and that Eps15 and Hrs are recruited by ubiquilin into ubiquitin-containing cytoplasmic aggregates. These results suggest that a ubiquitin network based upon interactions between UIM and UBL domains is involved in the clearance of intracellular protein aggregates.

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Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a UIM-UBL interaction

Elsa Regan-Klapisz, Irina Sorokina, Jarno Voortman, Peter de Keizer, Rob C. Roovers, Peter Verheesen, Sylvie Urbé, Lara Fallon, Edward A. Fon, Arie Verkleij, Alexandre Benmerah, and Paul M. P. van Bergen en Henegouwen
JCS 2005 118: 4437-4450. [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