EH domain-containing protein 1, also known as testilin or PAST homolog 1 (PAST1), is a protein that in humans is encoded by the EHD1gene[1] belonging to the EHD protein family.
This gene belongs to a highly conserved gene family encoding EPS15 homology (EH) domain-containing proteins. The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors.[1]
↑ 2.02.1Rotem-Yehudar, R; Galperin E; Horowitz M (Aug 2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". J. Biol. Chem. United States. 276 (35): 33054–60. doi:10.1074/jbc.M009913200. ISSN0021-9258. PMID11423532.
Further reading
Di Fiore PP, Pelicci PG, Sorkin A (1998). "EH: a novel protein-protein interaction domain potentially involved in intracellular sorting". Trends Biochem. Sci. 22 (11): 411–3. doi:10.1016/S0968-0004(97)01127-4. PMID9397678.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID8619474.
Mintz L, Galperin E, Pasmanik-Chor M, et al. (1999). "EHD1--an EH-domain-containing protein with a specific expression pattern". Genomics. 59 (1): 66–76. doi:10.1006/geno.1999.5800. PMID10395801.
Haider NB, Searby C, Galperin E, et al. (2000). "Evaluation and molecular characterization of EHD1, a candidate gene for Bardet-Biedl syndrome 1 (BBS1)". Gene. 240 (1): 227–32. doi:10.1016/S0378-1119(99)00395-9. PMID10564830.
Pohl U, Smith JS, Tachibana I, et al. (2000). "EHD2, EHD3, and EHD4 encode novel members of a highly conserved family of EH domain-containing proteins". Genomics. 63 (2): 255–62. doi:10.1006/geno.1999.6087. PMID10673336.
Rotem-Yehudar R, Galperin E, Horowitz M (2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". J. Biol. Chem. 276 (35): 33054–60. doi:10.1074/jbc.M009913200. PMID11423532.
Galperin E, Benjamin S, Rapaport D, et al. (2003). "EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1". Traffic. 3 (8): 575–89. doi:10.1034/j.1600-0854.2002.30807.x. PMID12121420.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID12665801.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Guilherme A, Soriano NA, Furcinitti PS, Czech MP (2004). "Role of EHD1 and EHBP1 in perinuclear sorting and insulin-regulated GLUT4 recycling in 3T3-L1 adipocytes". J. Biol. Chem. 279 (38): 40062–75. doi:10.1074/jbc.M401918200. PMID15247266.
Xu Y, Shi H, Wei S, et al. (2005). "Mutually exclusive interactions of EHD1 with GS32 and syndapin II". Mol. Membr. Biol. 21 (4): 269–77. doi:10.1080/09687680410001716871. PMID15371016.
Lee DW, Zhao X, Scarselletta S, et al. (2005). "ATP binding regulates oligomerization and endosome association of RME-1 family proteins". J. Biol. Chem. 280 (17): 17213–20. doi:10.1074/jbc.M412751200. PMID15710626.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID17081983.