The EH Network

The EH Network 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Experimental Cell Research Elsevier

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Publisher
Elsevier
Copyright
Copyright © 1999 Academic Press
ISSN
0014-4827
D.O.I.
10.1006/excr.1999.4694
Publisher site
See Article on Publisher Site

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.

Journal

Experimental Cell ResearchElsevier

Published: Nov 25, 1999

References

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    Mayer, B.J.
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  • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
    Sengar, A.S.; Wang, W.; Bishay, J.; Cohen, S.; Egan, S.E.
  • The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2
    Benmerah, A.; Gagnon, J.; Begue, B.; Megarbane, B.; Dautry-Varsat, A.; Cerf-Bensussan, N.
  • Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain
    Wigge, P.; Vallis, Y.; McMahon, H.T.
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  • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin–protein ligase gene RSP5
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    Wiley, H.S.
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    Lamaze, C.; Schmid, S.L.
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    Marsh, M.; Helenius, A.
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    Wendland, B.; Emr, S.D.; Riezman, H.
  • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
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