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Sci. STKE, 16 December 2003
Vol. 2003, Issue 213, p. re17
[DOI: 10.1126/stke.2132003re17]
REVIEWS
EH and UIM: Endocytosis and More
Simona Polo1,2,,
Stefano Confalonieri1,,
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.
Abstract:
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.
Interaction between Epsin/Yap180 Adaptors and the Scaffolds Ede1/Pan1 Is Required for Endocytosis.
L. Maldonado-Baez, M. R. Dores, E. M. Perkins, T. G. Drivas, L. Hicke, and B. Wendland (2008)
Mol. Biol. Cell
19, 2936-2948
|Abstract »|Full Text »|PDF »
An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor.
I. Roxrud, C. Raiborg, N. M. Pedersen, E. Stang, and H. Stenmark (2008)
J. Cell Biol.
180, 1205-1218
|Abstract »|Full Text »|PDF »
Site-specific ubiquitination exposes a linear motif to promote interferon-{alpha} receptor endocytosis.
K.G. S. Kumar, H. Barriere, C. J. Carbone, J. Liu, G. Swaminathan, P. Xu, Y. Li, D. P. Baker, J. Peng, G. L. Lukacs, et al. (2007)
J. Cell Biol.
179, 935-950
|Abstract »|Full Text »|PDF »
Caenorhabditis elegans Intersectin: A Synaptic Protein Regulating Neurotransmission.
S. Rose, M. G. Malabarba, C. Krag, A. Schultz, H. Tsushima, P. P. Di Fiore, and A. E. Salcini (2007)
Mol. Biol. Cell
18, 5091-5099
|Abstract »|Full Text »|PDF »
Decoding ubiquitin sorting signals for clathrin-dependent endocytosis by CLASPs.
Interactions between EHD Proteins and Rab11-FIP2: A Role for EHD3 in Early Endosomal Transport.
N. Naslavsky, J. Rahajeng, M. Sharma, M. Jovic, and S. Caplan (2006)
Mol. Biol. Cell
17, 163-177
|Abstract »|Full Text »|PDF »
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.
118, 4437-4450
|Abstract »|Full Text »|PDF »
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?.
,
Stefano Confalonieri1,
