ArticleMolecular biology of the cell2003
Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
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- Discovery of a rapidly evolving yeast defense factor,Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Adaptive laboratory evolution of β-caryophyllene producing Saccharomyces cerevisiae.Microbial cell factories · 2021Article
- Article
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- A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1.Journal of cell science · 2016Article
- A combined approach of quantitative interaction proteomics and live-cell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis.Molecular & cellular proteomics : MCP · 2013Article
- Rules for the recognition of dilysine retrieval motifs by coatomer.The EMBO journal · 2013Article
- Traffic COPs: rules of detection.The EMBO journal · 2013Article
- Statistical analysis reveals co-expression patterns of many pairs of genes in yeast are jointly regulated by interacting loci.PLoS genetics · 2013Article
- Review
- Gene expression network reconstruction by convex feature selection when incorporating genetic perturbations.PLoS computational biology · 2010Article
- Arf GAPs: gatekeepers of vesicle generation.FEBS letters · 2010Review
- Organization of physical interactomes as uncovered by network schemas.PLoS computational biology · 2008Article
- Global investigation of protein-protein interactions in yeast Saccharomyces cerevisiae using re-occurring short polypeptide sequences.Nucleic acids research · 2008Article
- The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus.The Journal of cell biology · 2008Article
- Novel cargo-binding site in the beta and delta subunits of coatomer.The Journal of cell biology · 2007Article
- Genotypic and physiological characterization of Saccharomyces boulardii, the probiotic strain of Saccharomyces cerevisiae.Applied and environmental microbiology · 2007Article
- Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins.Molecular and cellular biology · 2006Article
- Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth.The Journal of cell biology · 2005Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein trafficking is achieved by a bidirectional vesicle flow between the various compartments of the eukaryotic cell. COPII coated vesicles mediate anterograde protein transport from the endoplasmic reticulum to the Golgi apparatus, whereas retrograde Golgi-to-endoplasmic reticulum vesicles use the COPI coat. Inactivation of COPI vesicle formation in conditional sec21 (gamma-COP) mutants rapidly blocks transport of certain proteins along the early secretory pathway. We have identified the integral membrane protein Mst27p as a strong suppressor of sec21-3 and ret1-1 mutants. A C-terminal KKXX motif of Mst27p that allows direct binding to the COPI complex is crucial for its suppression ability. Mst27p and its homolog Yar033w (Mst28p) are part of the same complex. Both proteins contain cytoplasmic exposed C termini that have the ability to interact directly with COPI and COPII coat complexes. Site-specific mutations of the COPI binding domain abolished suppression of the sec21 mutants. Our results indicate that overexpression of MST27 provides an increased number of coat binding sites on membranes of the early secretory pathway and thereby promotes vesicle formation. As a consequence, the amount of cargo that can bind COPI might be important for the regulation of the vesicle flow in the early secretory pathway.
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