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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SNAP-associated protein

Snapin, SNAPAP
SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion (Ilardi et al., 1999 [PubMed 10195194]). SNAPAP is also a component of the ubiquitously expressed BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules (Starcevic and Dell'Angelica, 2004 [PubMed 15102850]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: SNAP-25, V1a, ACID, SNAP-23, DTNBP1
Papers on Snapin
Snapin interacts with G-protein coupled receptor PKR2.
Li et al., Changsha, China. In Biochem Biophys Res Commun, Feb 2016
In this study, we performed yeast two-hybrid screening by using PKR2 C-terminus (amino acids 333-384) as a bait, and identified Snapin as a novel interaction partner for PKR2.
Regulation of synaptic activity by snapin-mediated endolysosomal transport and sorting.
Sheng et al., Bethesda, United States. In Embo J, Sep 2015
Here, we used snapin mutants as tools to assess how endolysosomal sorting and trafficking impact presynaptic activity in wild-type and snapin(-/-) neurons.
Lower brain-derived neurotrophic factor levels associated with worsening fatigue in prostate cancer patients during repeated stress from radiation therapy.
Machado-Vieira et al., Bethesda, United States. In World J Biol Psychiatry, Apr 2015
This study investigated the association between plasma concentrations of three neurotrophic factors (BDNF, brain-derived neurotrophic factor; GDNF, glial-derived neurotrophic factor; and SNAPIN, soluble N-ethylmaleimide sensitive fusion attachment receptor-associated protein) and initial fatigue intensification during external beam radiation therapy (EBRT) in euthymic non-metastatic prostate cancer men.
Interaction between the human cytomegalovirus‑encoded UL142 and cellular Snapin proteins.
Ruan et al., Shenyang, China. In Mol Med Report, Feb 2015
A host protein, the SNARE‑associated protein Snapin, was identified to directly interact and colocalize with HCMV pUL142 in transfected human embryonic kidney‑293 cells.
Axonal autophagosomes use the ride-on service for retrograde transport toward the soma.
Sheng et al., Bethesda, United States. In Autophagy, 2014
Late endosome (LE)-loaded dynein-SNAPIN motor-adaptor complexes mediate the retrograde transport of autophagosomes upon their fusion with LEs in distal axons.
DRD1 rare variants associated with tardive-like dystonia: a pilot pathway sequencing study in dystonia.
Tijssen et al., Amsterdam, Netherlands. In Parkinsonism Relat Disord, 2014
We assessed all coding and non-coding variants in candidate genes in D1-like subclass of dopamine receptor genes (DRD1, DRD5) and the synaptic vesicle pathway linked to torsinA (TOR1A, STON2, SNAPIN, KLC1 and THAP1), spanning 96 Kb.
Chlamydia psittaci inclusion membrane protein IncB associates with host protein Snapin.
Hänel et al., Jena, Germany. In Int J Med Microbiol, 2014
Two-hybrid screening with the C. psittaci inclusion protein IncB as bait against a HeLa Yeast Two-hybrid (YTH) library revealed that the host protein Snapin interacts with IncB.
Snapin-mediated BACE1 retrograde transport is essential for its degradation in lysosomes and regulation of APP processing in neurons.
Cai et al., United States. In Cell Rep, 2014
Here, using snapin-deficient mice combined with gene rescue experiments, we reveal that Snapin, as a dynein motor adaptor for late endosomes, mediates BACE1 retrograde transport.
Modulation of the cellular distribution of human cytomegalovirus helicase by cellular factor Snapin.
Liu et al., Wuhan, China. In J Virol, 2013
In this study, we show that UL105 specifically interacts with Snapin, a human protein that is predominantly localized in the cytoplasm and associated with cellular vesicles.
LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25.
Seol et al., South Korea. In Exp Mol Med, 2012
Yeast two-hybrid screening revealed that Snapin, a SNAP-25 (synaptosomal-associated protein-25) interacting protein, interacts with LRRK2.
Snapin, positive regulator of stimulation- induced Ca²⁺ release through RyR, is necessary for HIV-1 replication in T cells.
Nolan et al., Suita, Japan. In Plos One, 2012
The target of one inhibitor peptide, Pep80, identified in this screen was determined to be Snapin, a protein associated with the soluble N-ethyl maleimide sensitive factor adaptor protein receptor (SNARE) complex that is critical for calcium-dependent exocytosis during neurotransmission.
SNAPIN: an endogenous Toll-like receptor ligand in rheumatoid arthritis.
Pope et al., Chicago, United States. In Ann Rheum Dis, 2012
These observations identify Snapin as a novel endogenous TLR2 ligand in rheumatoid arthritis, and thus support a role for persistent TLR2 signalling in pathogenesis.
Snapin is critical for presynaptic homeostatic plasticity.
Davis et al., San Francisco, United States. In J Neurosci, 2012
snapin functions in concert with dysbindin to modulate vesicle release and possibly homeostatic plasticity
Type VI adenylyl cyclase regulates neurite extension by binding to Snapin and Snap25.
Chern et al., Taipei, Taiwan. In Mol Cell Biol, 2011
AC6-mediated inhibition of neurite outgrowth was reversed by the overexpression of Snap25 or a Snapin mutant that could not be phosphorylated.
Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin.
Liu et al., Wuhan, China. In J Virol, 2011
These results suggest that Snapin may play a key role in regulating the cellular localization of human cytomegalovirus UL70, leading to modulation of viral DNA synthesis and progeny production.
Snapin mediates incretin action and augments glucose-dependent insulin secretion.
Hussain et al., Baltimore, United States. In Cell Metab, 2011
PKA-dependent phosphorylation of snapin increases interaction among insulin secretory vesicle-associated proteins, thereby potentiating glucose-stimulated insulin secretion.
Novel regulation of adenylyl cyclases by direct protein-protein interactions: insights from snapin and ric8a.
Chern et al., Taipei, Taiwan. In Neurosignals, 2008
Based on recent studies on AC-interacting proteins (particularly Snapin and Ric8a), this review focuses on the importance and possible involvement of AC-interacting proteins in (1) the association of the cAMP signaling pathway with various cellular machineries and (2) the coordination of tightly regulated cAMP signaling by other signaling molecules.
Regulation of the exocytotic machinery by cAMP-dependent protein kinase: implications for presynaptic plasticity.
Morgan et al., Liverpool, United Kingdom. In Biochem Soc Trans, 2003
Here we review two proteins that do fulfil these criteria: the synaptic vesicle proteins cysteine string protein (CSP) and Snapin.
Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex.
Sheng et al., Bethesda, United States. In Nat Cell Biol, 2001
Here we identify Snapin, a protein of relative molecular mass 15,000 that is implicated in neurotransmission by binding to SNAP-25, as a possible target.
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