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.
Exogenously and endogenously originated signals are propagated within the cell by functional and physical networks of proteins, leading to numerous biological outcomes. Many protein-protein interactions take place between binding domains and short peptide motifs. Frequently, these interactions are inducible by upstream signaling events, in which case one of the two binding surfaces may be created by a posttranslational modification. Here, we discuss two protein networks. One, the EH-network, is based on the Eps15 homology (EH) domain, which binds to peptides containing the sequence Asp-Pro-Phe (NPF). The other, which we define as the monoubiquitin (mUb) network, relies on monoubiquitination, which is emerging as an important posttranslational modification that regulates protein function. Both networks were initially implicated in the control of plasma membrane receptor endocytosis and in the regulation of intracellular trafficking routes. The ramifications of these two networks, however, appear to extend into many other aspects of cell physiology as well, such as transcriptional regulation, actin cytoskeleton remodeling, and DNA repair. The focus of this review is to integrate available knowledge of the EH- and mUb networks with predictions of genetic and physical interactions stemming from functional genomics approaches.
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?.