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Human SNPH Protein expressed in Escherichia coli (E. coli) - ABIN666869
Boczan, Leenders, Sheng: Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis. in The Journal of biological chemistry 2004
Show all 2 references for ABIN666869
syntaphilin is an inhibitor of both SNARE (show NAPA Proteins)-based fusion and dynamin (show DNM1 Proteins)-mediated endocytosis
SNPH deletion produces striking benefits in the Shiverer (show MBP Proteins) mouse by prolonging survival, reducing cerebellar damage, suppressing oxidative stress, and improving itochondrial health.
syntaphilin expression in astrocytes at the optic nerve might be involved in axonal injury.
SNPH is required for activity-dependent regulation of mitochondrial transport.
Here, we report a role for axon-targeted syntaphilin (SNPH) in mitochondrial docking through its interaction with microtubules. Axonal mitochondria that contain exogenously or endogenously expressed SNPH lose mobility.
Our studies suggest an unexpected role for LC8 (show DYNLL1 Proteins) and provide new mechanistic insights into how SNPH and LC8 (show DYNLL1 Proteins) together immobilize mitochondria through a dynamic interaction between the docking receptor and axonal cytoskeleton.
Syntaxin-1, synaptobrevin/VAMP, and SNAP25 interact to form the SNARE complex, which is required for synaptic vesicle docking and fusion. The protein encoded by this gene is membrane-associated and inhibits SNARE complex formation by binding free syntaxin-1. Expression of this gene appears to be brain-specific.