ArticleMolecular biology of the cell2011
Sec1p and Mso1p C-terminal tails cooperate with the SNAREs and Sec4p in polarized exocytosis.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- The Ync13-Rga7-Rng10 complex selectively coordinates secretory vesicle trafficking and secondary septum formation during cytokinesis.PLoS biology · 2025Article
- Spatial control of secretory vesicle targeting by the Ync13-Rga7-Rng10 complex during cytokinesis.bioRxiv : the preprint server for biology · 2025Article
- Bimolecular Fluorescence Complementation (BiFC) Technique for Exocytic Proteins in Murine Hippocampal Neurons.Methods in molecular biology (Clifton, N.J.) · 2025Article
- High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane ineLife · 2022Article
- Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis.Molecular biology of the cell · 2020Article
- A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions.Molecular biology of the cell · 2013Article
- Myosin-V is activated by binding secretory cargo and released in coordination with Rab/exocyst function.Developmental cell · 2012Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.The EMBO journal · 2012Article
- Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.Molecular biology of the cell · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Sec1/Munc18 protein family members perform an essential, albeit poorly understood, function in association with soluble n-ethylmaleimide sensitive factor adaptor protein receptor (SNARE) complexes in membrane fusion. The Saccharomyces cerevisiae Sec1p has a C-terminal tail that is missing in its mammalian homologues. Here we show that deletion of the Sec1p tail (amino acids 658-724) renders cells temperature sensitive for growth, reduces sporulation efficiency, causes a secretion defect, and abolishes Sec1p-SNARE component coimmunoprecipitation. The results show that the Sec1p tail binds preferentially ternary Sso1p-Sec9p-Snc2p complexes and it enhances ternary SNARE complex formation in vitro. The bimolecular fluorescence complementation (BiFC) assay results suggest that, in the SNARE-deficient sso2-1 Δsso1 cells, Mso1p, a Sec1p binding protein, helps to target Sec1p(1-657) lacking the C-terminal tail to the sites of secretion. The results suggest that the Mso1p C terminus is important for Sec1p(1-657) targeting. We show that, in addition to Sec1p, Mso1p can bind the Rab-GTPase Sec4p in vitro. The BiFC results suggest that Mso1p acts in close association with Sec4p on intracellular membranes in the bud. This association depends on the Sec4p guanine nucleotide exchange factor Sec2p. Our results reveal a novel binding mode between the Sec1p C-terminal tail and the SNARE complex, and suggest a role for Mso1p as an effector of Sec4p.
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