Article

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

National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Genome biology (Impact Factor: 10.47). 02/2002; 3(5):research0023. DOI: 10.1186/gb-2002-3-5-research0023
Source: PubMed

ABSTRACT 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.
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.
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.

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Available from: Vivek Anantharaman, Jul 27, 2015
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    • "Indeed it has been proposed that oligomerization is required for the proper localization of p24 proteins (Emery et al., 2000; Ciufo and Boyd, 2000). The luminal GOLD domain, present in several proteins involved in Golgi dynamics, is predicted to be involved in specific protein–protein interactions and has been postulated to interact with putative cargo proteins (Anantharaman and Aravind, 2002; Carney and Bowen, 2004). "
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    ABSTRACT: p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)-p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in Arabidopsis root tip cells by immunogold electron microscopy. The relative contributions of the cytosolic tail and the luminal domains to p24δ5 trafficking have also been characterized. It is demonstrated that whereas the dilysine motif in the cytoplasmic tail determines the location of p24δ5 in the early secretory pathway, the luminal domain may contribute to its distribution downstream of the Golgi apparatus. By using knock-out mutants and co-immunoprecipitation experiments, it is shown that p24δ5 and p24β2 interact with each other. Finally, it is shown that p24δ5 and p24β2 exhibit coupled trafficking at the ER-Golgi interface. It is proposed that p24δ5 and p24β2 interact with each other at ER export sites for ER exit and coupled transport to the Golgi apparatus. Once in the Golgi, p24δ5 interacts very efficiently with the COPI machinery for retrograde transport back to the ER.
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    • "The GOLD domain is typically 90–150 aa long and folds into six or seven b-strands. This domain has been identified in several proteins with roles in Golgi dynamics and secretion including p24 proteins and Sec14 proteins, and is thought to serve as a common denominator in protein–protein interactions (Anantharaman and Aravind, 2002). It would be interesting to investigate whether the AiV proteins have the ability to bind to other GOLD domain-containing proteins. "
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    • "CRAL/TRIO domains form hydrophobic binding pockets that bind small hydrophobic ligands (Bateman et al., 2000; Sha et al., 1998; Stocker et al., 2002; Stocker and Baumann, 2003; Panagabko et al., 2003). GOLD (Golgi dynamics) domains were identified by protein alignments and are of unknown function (Stocker et al., 2002; Anantharaman and Aravind, 2002). "
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