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The EH Network
Abstract
The EH domain is an evolutionary conserved protein-protein interaction domain present in a growing number of proteins from yeast to mammals. Even though the domain was discovered just 5 years ago, a great deal has been learned regarding its three-dimensional structure and binding specificities. Moreover, a number of cellular ligands of the domain have been identified and demonstrated to define a complex network of protein-protein interactions in the eukaryotic cell. Interestingly, many of the EH-containing and EH-binding proteins display characteristics of endocytic "accessory" proteins, suggesting that the principal function of the EH network is to regulate various steps in endocytosis. In addition, recent evidence suggests that the EH network might work as an "integrator" of signals controlling cellular pathways as diverse as endocytosis, nucleocytosolic export, and ultimately cell proliferation.
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Mammalian EH domain-containing proteins include eps15, intersectin, POB-1 and EHD1.
“Mammalian EH domain-containing proteins include eps15, intersectin, POB-1 and EHD1 (Santolini et al., 1999).”
From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Santolini et al., 1999
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Gaullier, J.-M., Simonsen, A., D'Arrigo, A., Bremnes, B., Stenmark, H., & Aasland, R. (1998) · Nature · doi:10.1038/28767 · Cited by 553
Chen, H., Slepnev, V. I., Di Fiore, P. P., & De Camilli, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3257 · Cited by 138 · cited 5×
“It was shown that, like ps15, Epsin undergoes depolarization-dependent dehosphorylation in nerve terminals and that dephoshorylation enhances the association with AP-2 in rain extracts [46].”
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Metadata
- Authors
- Santolini, E., Salcini, A. E., Kay, B. K., Yamabhai, M., & Di Fiore, P. P.
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 253
- Issue
- 1
- Pages
- 186-209
- ISSN
- 0014-4827
- Cited by
- 111
- References
- 2
- Language
- en
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