The GOLD domain, a novel protein module involved in Golgi function and secretion.
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.
Anantharaman
Vivek
V
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Aravind
L
L
D000595:Amino Acid Sequence / Q000235:genetics / Q000502:physiology; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology; D019295:Computational Biology / Q000379:methods; D017124:Conserved Sequence / Q000235:genetics / Q000502:physiology; D030562:Databases, Protein; D004721:Endoplasmic Reticulum / Q000378:metabolism / Q000502:physiology; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D006056:Golgi Apparatus / Q000378:metabolism* / Q000502:physiology*; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D021381:Protein Transport / Q000235:genetics / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; C093262:EMP24 protein, S cerevisiae; C053330:Golgi membrane glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins