gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.


syntaphilin, SNPH
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, OUT, Dynamin I, SNAP-25, Synaptobrevin
Papers on syntaphilin
Deletion of mitochondrial anchoring protects dysmyelinating shiverer: implications for progressive MS.
Chiu et al., Bethesda, United States. In J Neurosci, May 2015
In this study, we identified various parallelisms between progressive MS and the dysmyelinating mouse model Shiverer and then genetically deleted a major neuron-specific mitochondrial anchoring protein Syntaphilin (SNPH) from the mouse.
The expression of syntaphilin is down-regulated in the optic nerve after axonal injury.
Negi et al., Kōbe, Japan. In Exp Eye Res, 2014
Syntaphilin was recently discovered as a docking protein that affects mitochondrial mobility.
Differentiation state-specific mitochondrial dynamic regulatory networks are revealed by global transcriptional analysis of the developing chicken lens.
Kantorow et al., Boca Raton, United States. In G3 (bethesda), 2014
These included differences in the expression levels of metabolic (DUT, PDK1, SNPH), autophagy (ATG3, ATG4B, BECN1, FYCO1, WIPI1), and mitophagy (BNIP3L/NIX, BNIP3, PARK2, p62/SQSTM1) transcripts between lens epithelial cells and lens fiber cells.
Mitochondrial immobilization mediated by syntaphilin facilitates survival of demyelinated axons.
Trapp et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2014
We show that the axonal mitochondrial volume increase following acute demyelination of WT CNS axons does not occur in demyelinated axons deficient in syntaphilin, an axonal molecule that immobilizes stationary mitochondria to microtubules.
Motile axonal mitochondria contribute to the variability of presynaptic strength.
Sheng et al., Bethesda, United States. In Cell Rep, 2013
Recently, we identified syntaphilin as an axonal mitochondrial-docking protein.
Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport.
Sheng et al., Bethesda, United States. In J Cell Biol, 2013
In this paper, using genetic mouse model combined with live imaging, we demonstrate that syntaphilin (SNPH) mediates the activity-dependent immobilization of axonal mitochondria through binding to KIF5.
Dynein c1h1, dynactin and syntaphilin expression in brain areas related to neurodegenerative diseases following exposure to rotenone.
Ferrari et al., São Paulo, Brazil. In Acta Neurobiol Exp (wars), 2012
The effects of low concentrations of rotenone on the expression of dynein c1h1, dynactin and syntaphilin, which are proteins related to mitochondria transport and anchoring, were evaluated in cell cultures of substantia nigra, locus coeruleus and hippocampus as well as in these same brain areas in Lewis aged rats.
Candidate pathway association study in cocaine dependence: the control of neurotransmitter release.
Ribasés et al., Barcelona, Spain. In World J Biol Psychiatry, 2012
We examined the possible contribution to cocaine dependence of 16 genes involved in the cellular machinery that controls neurotransmitter release: genes encoding proteins of the SNARE complex (STX1A, SNAP25, VAMP1 and VAMP2), fusion control elements (SYT1, SYT2, CPLX1, CPLX2, CPLX3 and CPLX4) and regulatory elements (STXBP1, SYP, SNPH, NSF, NAPA and RAB3A).
Increased axonal mitochondrial mobility does not slow amyotrophic lateral sclerosis (ALS)-like disease in mutant SOD1 mice.
Sheng et al., Bethesda, United States. In J Biol Chem, 2011
Using genetic mouse models combined with time-lapse imaging of live neurons, we previously discovered that axon-targeted syntaphilin (SNPH) acts as a docking receptor specific for axonal mitochondria.
Dynein light chain LC8 regulates syntaphilin-mediated mitochondrial docking in axons.
Sheng et al., Bethesda, United States. In J Neurosci, 2009
Our studies suggest an unexpected role for LC8 and provide new mechanistic insights into how SNPH and LC8 together immobilize mitochondria through a dynamic interaction between the docking receptor and axonal cytoskeleton.
Mitochondrial changes within axons in multiple sclerosis.
Turnbull et al., Newcastle upon Tyne, United Kingdom. In Brain, 2009
The axon-specific mitochondrial docking protein (syntaphilin) and phosphorylated neurofilament-H were increased in chronic lesions.
Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation.
Sheng et al., Bethesda, United States. In Cell, 2008
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.
Cerebrospinal fluid markers before and after shunting in patients with secondary and idiopathic normal pressure hydrocephalus.
Wikkelsö et al., Göteborg, Sweden. In Cerebrospinal Fluid Res, 2007
METHODS: We measured clinical symptoms and analysed lumbar CSF for protein content, neurodegeneration and neurotransmission markers in patients with secondary (SNPH, n = 17) and idiopathic NPH (INPH, n = 18) before and 3 months after shunt surgery.
Molecular cloning of the m-Golsyn gene and its expression in the mouse brain.
Ito et al., Hirakata, Japan. In Gene Expr, 2005
m-Golsyn protein was found to be homologous to syntaphilin, a regulator of synaptic vesicle exocytosis.
Molecular cloning and characterization of gene for Golgi-localized syntaphilin-related protein on human chromosome 8q23.
Ito et al., Hirakata, Japan. In Gene, 2005
Furthermore, these proteins were homologous to syntaphilin, a molecule involved in guiding vesicular transport.
Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis.
Sheng et al., Bethesda, United States. In J Biol Chem, 2004
syntaphilin was identified as a molecular clamp that controls free syntaxin-1 and dynamin-1 availability and thereby regulates synaptic vesicle exocytosis and endocytosis. PKA phosphorylation of syntaphilin decreases its binding to syntaxin-1A in vitro.
Syntaphilin binds to dynamin-1 and inhibits dynamin-dependent endocytosis.
Sheng et al., Bethesda, United States. In J Biol Chem, 2003
syntaphilin is an inhibitor of both SNARE-based fusion and dynamin-mediated endocytosis
share on facebooktweetadd +1mail to friends