ArticleMolecular biology of the cell1999
Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Exocytosis Proteins: Typical and Atypical Mechanisms of Action in Skeletal Muscle.Frontiers in endocrinology · 2022Review
- The nuts and bolts of the platelet release reaction.Platelets · 2017Review
- Article
- Vesicle-associated membrane protein-2 (VAMP2) mediates cAMP-stimulated renin release in mouse juxtaglomerular cells.The Journal of biological chemistry · 2011Article
- Rapid phosphorylation of a syntaxin during the Avr9/Cf-9-race-specific signaling pathway.Plant physiology · 2005Article
- EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.Molecular biology of the cell · 2005Article
- The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machinery.Molecular biology of the cell · 2005Article
- Phosphorylation of SNAP-25 on serine-187 is induced by secretagogues in insulin-secreting cells, but is not correlated with insulin secretion.The Biochemical journal · 2002Article
- t-SNARE phosphorylation regulates endocytosis in yeast.Molecular biology of the cell · 2002Article
- Genomic analysis of homotypic vacuole fusion.Molecular biology of the cell · 2002Article
- t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast.The EMBO journal · 2001Article
- Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery.Molecular biology of the cell · 2000Article
- A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The docking and fusion of cargo-containing vesicles with target membranes of eukaryotic cells is mediated by the interaction of SNARE proteins present on both vesicle and target membranes. In many cases, the target membrane SNARE, or t-SNARE, exists as a complex of syntaxin with a member of the SNAP-25 family of palmitoylated proteins. We have identified a novel human kinase SNAK (SNARE kinase) that specifically phosphorylates the nonneuronal t-SNARE SNAP-23 in vivo. Interestingly, only SNAP-23 that is not assembled into t-SNARE complexes is phosphorylated by SNAK, and phosphorylated SNAP-23 resides exclusively in the cytosol. Coexpression with SNAK significantly enhances the stability of unassembled SNAP-23, and as a consequence, the assembly of newly synthesized SNAP-23 with syntaxin is augmented. These data demonstrate that phosphorylation of SNAP-23 by SNAK enhances the kinetics of t-SNARE assembly in vivo.
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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.