Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Sci. STKE, 16 December 2003
Vol. 2003, Issue 213, p. re17
EH and UIM: Endocytosis and More
Anna Elisabetta Salcini1,2, and
Pier Paolo Di Fiore1,2,3*
1Istituto FIRC di Oncologia Molecolare, Via Adamello 16, 20139 Milan, Italy. 2Istituto Europeo di Oncologia, Via Ripamonti 435, 20141 Milan, Italy. 3University of Milan, Medical School, 20122 Milan, Italy. S.P. and S.C. contributed equally.
Gloss: This STKE Review, with 4 figures, 7 tables, and 181 references, concerns protein interaction networks built through two classes of protein-protein interactions, those involving the Eps15 homology (EH) domain and those that depend on monoubiquitination, a posttranslational modification that creates the monoubiquitin (mUb)-network. Functional and physical protein networks linked by protein interaction domains--regions with conserved structure and amino acid sequence--can be created through signaling events and serve functions critical to intracellular signaling pathways. The protein networks involving EH domains and ubiquitin (Ub)-interacting motifs (UIMs) were initially implicated in the regulation of receptor endocytosis and in the trafficking of intracellular vesicles. More recent data, however, indicate that both networks serve other important functions as well. This review integrates available knowledge on the EH- and mUb networks with predictions based on functional genomics.
Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a UIM-UBL interaction.
E. Regan-Klapisz, I. Sorokina, J. Voortman, P. de Keizer, R. C. Roovers, P. Verheesen, S. Urbe, L. Fallon, E. A. Fon, A. Verkleij, et al. (2005)
J. Cell Sci.
|Abstract »|Full Text »|PDF »
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?.