The EH network
- PMID: 10579923
- DOI: 10.1006/excr.1999.4694
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.
Copyright 1999 Academic Press.
Similar articles
-
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?J Cell Sci. 2005 Sep 15;118(Pt 18):4093-101. doi: 10.1242/jcs.02595. J Cell Sci. 2005. PMID: 16155252
-
The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport.J Cell Biol. 1999 Dec 27;147(7):1379-84. doi: 10.1083/jcb.147.7.1379. J Cell Biol. 1999. PMID: 10613896 Free PMC article.
-
Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites.Biochemistry. 2000 Apr 18;39(15):4309-19. doi: 10.1021/bi9927383. Biochemistry. 2000. PMID: 10757979
-
The Eps15 homology (EH) domain.FEBS Lett. 2002 Feb 20;513(1):24-9. doi: 10.1016/s0014-5793(01)03241-0. FEBS Lett. 2002. PMID: 11911876 Review.
-
Endocytosis: EH domains lend a hand.Curr Biol. 1999 Jan 28;9(2):R70-3. doi: 10.1016/s0960-9822(99)80014-1. Curr Biol. 1999. PMID: 10021353 Review.
Cited by
-
The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae.Genetics. 2003 Dec;165(4):1661-74. doi: 10.1093/genetics/165.4.1661. Genetics. 2003. PMID: 14704157 Free PMC article.
-
Cep57, a multidomain protein with unique microtubule and centrosomal localization domains.Biochem J. 2008 Jun 1;412(2):265-73. doi: 10.1042/BJ20071501. Biochem J. 2008. PMID: 18294141 Free PMC article.
-
Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor.EMBO J. 2002 Sep 16;21(18):4915-26. doi: 10.1093/emboj/cdf487. EMBO J. 2002. PMID: 12234931 Free PMC article.
-
Cellular functions and intrinsic attributes of the ATP-binding Eps15 homology domain-containing proteins.Protein Sci. 2020 Jun;29(6):1321-1330. doi: 10.1002/pro.3860. Epub 2020 Apr 11. Protein Sci. 2020. PMID: 32223019 Free PMC article. Review.
-
Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis.J Cell Biol. 2000 Aug 21;150(4):905-12. doi: 10.1083/jcb.150.4.905. J Cell Biol. 2000. PMID: 10953014 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases