The GOLD domain, a novel protein module involved in Golgi function and secretion. Export

@article{citeulike:2926144, abstract = {BACKGROUND: Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have been shown to be critical components of the coated vesicles that are involved in the transportation of cargo molecules from the endoplasmic reticulum to the Golgi complex. The p24 proteins form hetero-oligomeric complexes and are believed to function as receptors for specific secretory cargo. RESULTS: Using sensitive sequence-profile analysis methods, we identified a novel beta-strand-rich domain, the GOLD (Golgi dynamics) domain, in the p24 proteins and several other proteins with roles in Golgi dynamics and secretion. This domain is predicted to mediate diverse protein-protein interactions. Other than in the p24 proteins, the GOLD domain is always found combined with lipid- or membrane-association domains such as the pleckstrin homology (PH), Sec14p and FYVE domains. CONCLUSIONS: The identification of the GOLD domain could aid in directed investigation of the role of the p24 proteins in the secretion process. The newly detected group of GOLD-domain proteins, which might simultaneously bind membranes and other proteins, point to the existence of a novel class of adaptors that could have a role in the assembly of membrane-associated complexes or in regulating assembly of cargo into membranous vesicles.}, address = {National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.}, author = {Anantharaman, V. and Aravind, L.}, citeulike-article-id = {2926144}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12049664}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12049664}, issn = {1465-6914}, journal = {Genome biology}, keywords = {conform\_change, golgi, in\_vivo, interactions, membrane, p24\_family, protein, vesicle}, number = {5}, posted-at = {2008-06-25 16:26:34}, priority = {2}, title = {The GOLD domain, a novel protein module involved in Golgi function and secretion.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12049664}, volume = {3}, year = {2002} }

TY - JOUR ID - citeulike:2926144 L3 - citeulike-article-id:2926144 N2 - BACKGROUND: Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have been shown to be critical components of the coated vesicles that are involved in the transportation of cargo molecules from the endoplasmic reticulum to the Golgi complex. The p24 proteins form hetero-oligomeric complexes and are believed to function as receptors for specific secretory cargo. RESULTS: Using sensitive sequence-profile analysis methods, we identified a novel beta-strand-rich domain, the GOLD (Golgi dynamics) domain, in the p24 proteins and several other proteins with roles in Golgi dynamics and secretion. This domain is predicted to mediate diverse protein-protein interactions. Other than in the p24 proteins, the GOLD domain is always found combined with lipid- or membrane-association domains such as the pleckstrin homology (PH), Sec14p and FYVE domains. CONCLUSIONS: The identification of the GOLD domain could aid in directed investigation of the role of the p24 proteins in the secretion process. The newly detected group of GOLD-domain proteins, which might simultaneously bind membranes and other proteins, point to the existence of a novel class of adaptors that could have a role in the assembly of membrane-associated complexes or in regulating assembly of cargo into membranous vesicles. IS - 5 JF - Genome biology SN - 1465-6914 AD - National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. TI - The GOLD domain, a novel protein module involved in Golgi function and secretion. VL - 3 KW - conform_change KW - golgi KW - in_vivo KW - interactions KW - membrane KW - p24_family KW - protein KW - vesicle AU - Anantharaman, V AU - Aravind, L PY - 2002/// UR - http://view.ncbi.nlm.nih.gov/pubmed/12049664 ER -