ArticleJournal of cell science2009
Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism.
Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026Review
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Cargo selective vesicle tethering: The structural basis for binding of specific cargo proteins by the Golgi tether component TBC1D23.Science advances · 2024Article
- Transport mechanisms between the endocytic, recycling, and biosynthetic pathways via endosomes and theFrontiers in cell and developmental biology · 2024Review
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- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- Endocytic trafficking factor VPS45 is essential for spatial regulation of lens fiber differentiation in zebrafish.Development (Cambridge, England) · 2018Article
- The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation.Frontiers in cell and developmental biology · 2016Review
- Syntaxin 16 is a master recruitment factor for cytokinesis.Molecular biology of the cell · 2013Article
- Sorting of GLUT4 into its insulin-sensitive store requires the Sec1/Munc18 protein mVps45.Molecular biology of the cell · 2013Article
- Endosomal sorting of GLUT4 and Gap1 is conserved between yeast and insulin-sensitive cells.Journal of cell science · 2013Article
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- The role of Munc18-1 and its orthologs in modulation of cortical F-actin in chromaffin cells.Journal of molecular neuroscience : MN · 2012Review
- The Sec1/Munc18 protein Vps45 regulates cellular levels of its SNARE binding partners Tlg2 and Snc2 in Saccharomyces cerevisiae.PloS one · 2012Article
- Organization of SNAREs within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011Review
- The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane fusion in all eukaryotic cells is regulated by the formation of specific SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complexes. The molecular mechanisms that control this process are conserved through evolution and require several protein families, including Sec1p/Munc18 (SM) proteins. Here, we demonstrate that the mammalian SNARE protein syntaxin 16 (Sx16, also known as Syn16) is a functional homologue of the yeast SNARE Tlg2p, in that its expression fully complements the mutant phenotypes of tlg2Delta mutant yeast. We have used this functional homology to demonstrate that, as observed for Tlg2p, the function of Sx16 is regulated by the SM protein Vps45p. Furthermore, in vitro SNARE-complex assembly studies demonstrate that the N-terminal domain of Tlg2p is inhibitory to the formation of SNARE complexes, and that this inhibition can be lifted by the addition of purified Vps45p. By combining these cell-biological and biochemical analyses, we propose an evolutionarily conserved regulatory mechanism for Vps45p function. Our data support a model in which the SM protein is required to facilitate a switch of Tlg2p and Sx16 from a closed to an open conformation, thus allowing SNARE-complex assembly and membrane fusion to proceed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.