Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. This domain corresponds closely to the beta-strand rich GOLD domain described in (PUBMED:12049664). The GOLD domain is always found combined with lipid- or membrane-association domains (PUBMED:12049664).
The GOLD (for Golgi dynamics) domain is a protein module found in several eukaryotic Golgi and lipid-traffic proteins. It is typically between 90 and 150 amino acids long. Most of the size difference observed in the GOLD-domain superfamily is traceable to a single large low-complexity insert that is seen in some versions of the domain. With the exception of the p24 proteins, which have a simple architecture with the GOLD domain as their only globular domain, all other GOLD-domain proteins contain additional conserved globular domains. In these proteins, the GOLD domain co-occurs with lipid-, sterol- or fatty acid-binding domains such as PH, CRAL-TRIO, FYVE oxysterol binding- and acyl CoA-binding domains, suggesting that these proteins may interact with membranes. The GOLD domain can also be found associated with a RUN domain, which may have a role in the interaction of various proteins with cytoskeletal filaments. The GOLD domain is predicted to mediate diverse protein-protein interactions [ (PUBMED:12049664) ]. A secondary structure prediction for the GOLD domain reveals that it is likely to adopt a compact all-beta-fold structure with six to seven strands. Most of the sequence conservation is centred on the hydrophobic cores that support these predicted strands. The predicted secondary-structure elements and the size of the conserved core of the domain suggests that it may form a beta- sandwich fold with the strands arranged in two beta sheets stacked on each other [ (PUBMED:12049664) ].
Some proteins known to contain a GOLD domain are listed below:
Eukaryotic proteins of the p24 family.
Animal Sec14-like proteins. They are involved in secretion.
Human Golgi resident protein GCP60. It interacts with the Golgi integral membrane protein Giantin.
Yeast oxysterol-binding protein homologue 3 (OSH3).
Family alignment:
There are 9982 EMP24_GP25L domains in 9973 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing EMP24_GP25L domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with EMP24_GP25L domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing EMP24_GP25L domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
The GOLD domain, a novel protein module involved in Golgi function and secretion.
Genome Biol. 2002; 3: 23-23
Display abstract
BACKGROUND: Members of the p24 (p24/gp25L/emp24/Erp) family of proteins have beenshown to be critical components of the coated vesicles that are involved in thetransportation of cargo molecules from the endoplasmic reticulum to the Golgicomplex. The p24 proteins form hetero-oligomeric complexes and are believed tofunction as receptors for specific secretory cargo. RESULTS: Using sensitivesequence-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 mediatediverse protein-protein interactions. Other than in the p24 proteins, the GOLDdomain is always found combined with lipid- or membrane-association domains such as the pleckstrin homology (PH), Sec14p and FYVE domains. CONCLUSIONS: Theidentification of the GOLD domain could aid in directed investigation of the roleof the p24 proteins in the secretion process. The newly detected group ofGOLD-domain proteins, which might simultaneously bind membranes and otherproteins, point to the existence of a novel class of adaptors that could have arole in the assembly of membrane-associated complexes or in regulating assemblyof cargo into membranous vesicles.
gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP Iand II coatomer.
J Cell Biol. 1998; 140: 751-65
Display abstract
Abstract. Five mammalian members of the gp25L/ emp24/p24 family have beenidentified as major constituents of the cis-Golgi network of rat liver and HeLacells. Two of these were also found in membranes of higher density (correspondingto the ER), and this correlated with their ability to bind COP I in vitro. Thisbinding was mediated by a K(X)KXX-like retrieval motif present in the cytoplasmicdomain of these two members. A second motif, double phenylalanine (FF), presentin the cytoplasmic domain of all five members, was shown to participate in thebinding of Sec23 (COP II). This motif is part of a larger one, similar to theF/YXXXXF/Y strong endocytosis and putative AP2 binding motif. In vivo mutational analysis confirmed the roles of both motifs so that when COP I binding wasexpected to be impaired, cell surface expression was observed, whereas mutationof the Sec23 binding motif resulted in a redistribution to the ER. Surprisingly, upon expression of mutated members, steady-state distribution of unmutated onesshifted as well, presumably as a consequence of their observed oligomericproperties.
