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

Synaptosomal-associated protein, 29kDa

soluble NSF attachment protein, SNAP29, GS32
This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle membrane docking and fusion to the plasma membrane. The protein encoded by this gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found free in the cytoplasm. Use of multiple polyadenylation sites has been noted for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: NSF, SNAP-25, CAN, Synaptobrevin, abi1
Papers on soluble NSF attachment protein
Establishment of two mouse models for CEDNIK syndrome reveals the pivotal role of SNAP29 in epidermal differentiation.
Emmert et al., Göttingen, Germany. In J Invest Dermatol, Jan 2016
UNASSIGNED: Loss-of-function mutations in the SNAP29 gene cause CEDNIK (CErebral Dysgenesis, Neuropathy, Ichthyosis, Keratoderma) syndrome.
Identification of roles for the SNARE-associated protein, SNAP29, in mouse platelets.
Poole et al., Cambridge, United Kingdom. In Platelets, Dec 2015
SNAP29 is a tSNARE found in platelets, but whose role has not been defined.
Cargo-selective apical exocytosis in epithelial cells is conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3.
Huber et al., Innsbruck, Austria. In J Cell Biol, Dec 2015
Mutations in the motor protein Myosin Vb (Myo5B) or the soluble NSF attachment protein receptor Syntaxin 3 (Stx3) disturb epithelial polarity and cause microvillus inclusion disease (MVID), a lethal hereditary enteropathy affecting neonates.
Computer-aided identification, synthesis, and biological evaluation of novel inhibitors for botulinum neurotoxin serotype A.
Swaminathan et al., Stony Brook, United States. In Bioorg Med Chem, Oct 2015
BoNTs have been shown to block neurotransmitter release by cleaving proteins of the soluble NSF attachment protein receptor (SNARE) complex.
ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes.
Zhong et al., Stanford, United States. In Nature, May 2015
Here we report that ATG14 (also known as beclin-1-associated autophagy-related key regulator (Barkor) or ATG14L), an essential autophagy-specific regulator of the class III phosphatidylinositol 3-kinase complex, promotes membrane tethering of protein-free liposomes, and enhances hemifusion and full fusion of proteoliposomes reconstituted with the target (t)-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) syntaxin 17 (STX17) and SNAP29, and the vesicle (v)-SNARE VAMP8 (vesicle-associated membrane protein 8).
Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.
Yoon et al., Taejŏn, South Korea. In Science, Apr 2015
During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (α-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex for recycling of the SNARE proteins.
Role of cholesterol in SNARE-mediated trafficking on intracellular membranes.
Grewal et al., Barcelona, Spain. In J Cell Sci, Apr 2015
This process is not only driven by several soluble NSF attachment protein (SNAP) receptor (SNARE) proteins, which are key players in vesicle transport at the cell surface and intracellular compartments, but is also tightly modulated by cholesterol.
Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary vesicle formation.
Westlake et al., Frederick, United States. In Nat Cell Biol, Mar 2015
SNAP29, a SNARE membrane fusion regulator and EHD1-binding protein, is also required for DAV-mediated ciliary vesicle assembly.
Mechanistic insights into the recycling machine of the SNARE complex.
Brunger et al., Stanford, United States. In Nature, Mar 2015
The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion.
The proteins of exocytosis: lessons from the sperm model.
Tomes, Mendoza, Argentina. In Biochem J, Mar 2015
The proteins involved in these processes belong to several highly conserved families: Rab GTPases, SNAREs (soluble NSF-attachment protein receptors), α-SNAP (α-NSF attachment protein), NSF (N-ethylmaleimide-sensitive factor), Munc13 and -18, complexins and synaptotagmins.
Cortical Granule Exocytosis Is Mediated by Alpha-SNAP and N-Ethilmaleimide Sensitive Factor in Mouse Oocytes.
Michaut et al., Mendoza, Argentina. In Plos One, 2014
The molecular mechanism of membrane fusion during CGE is still poorly understood and is thought to be mediated by the SNARE pathway; nevertheless, it is unkown if SNAP (acronym for soluble NSF attachment protein) and NSF (acronym for N-ethilmaleimide sensitive factor), two key proteins in the SNARE pathway, mediate CGE in any oocyte model.
Sugar modification inhibits autophagosome-lysosome fusion.
Mizushima, Tokyo, Japan. In Nat Cell Biol, 2014
A genetic screen in Caenorhabditis elegans revealed that O-linked N-acetylglucosamine modification of the SNARE protein SNAP-29 negatively regulates SNARE-dependent fusion between autophagosomes and lysosomes.
The dendritic SNARE fusion machinery involved in AMPARs insertion during long-term potentiation.
Jurado, Baltimore, United States. In Front Cell Neurosci, 2013
Increasing evidence suggests that similarly to neurotransmitter release, AMPARs insertion relies on the formation of a SNARE complex (soluble NSF-attachment protein receptor), whose composition in dendrites has just begun to be elucidated.
Evolutionarily conserved role and physiological relevance of a STX17/Syx17 (syntaxin 17)-containing SNARE complex in autophagosome fusion with endosomes and lysosomes.
Juhász et al., Budapest, Hungary. In Autophagy, 2013
Two recent papers conclude that STX17/syntaxin 17 (Syx17 in Drosophila) has an evolutionarily conserved role in autophagosome fusion with endosomes and lysosomes, acting in one SNARE complex with SNAP29 (ubisnap in Drosophila) and the endosomal/lysosomal VAMP8 (CG1599/Vamp7 in Drosophila).
CORVET and HOPS tethering complexes - coordinators of endosome and lysosome fusion.
Ungermann et al., Osnabrück, Germany. In J Cell Sci, 2013
Both complexes are heterohexamers; they share four subunits, interact with Rab GTPases and soluble NSF attachment protein receptors (SNAREs) and can tether membranes.
CEDNIK syndrome results from loss-of-function mutations in SNAP29.
Sprecher et al., Tel Aviv-Yafo, Israel. In Br J Dermatol, 2011
a causal relationship between defective function of SNAP29 and the pleiotropic manifestations of CEDNIK syndrome
Loss of SNAP29 impairs endocytic recycling and cell motility.
Horowitz et al., Tel Aviv-Yafo, Israel. In Plos One, 2009
SNAP29 mediated membrane fusion has an important role in endocytic recycling and consequently, in cell motility
A mutation in SNAP29, coding for a SNARE protein involved in intracellular trafficking, causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma.
Mandel et al., Haifa, Israel. In Am J Hum Genet, 2005
a SNAP29 mutation codes for a SNARE protein involved in intracellular trafficking and causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma
SNAP-29-mediated modulation of synaptic transmission in cultured hippocampal neurons.
Sheng et al., Shanghai, China. In J Biol Chem, 2005
SNAP-29 acts as a negative modulator for neurotransmitter release, probably by slowing recycling of the SNARE-based fusion machinery and synaptic vesicle turnover
Mutually exclusive interactions of EHD1 with GS32 and syndapin II.
Hong et al., Singapore, Singapore. In Mol Membr Biol, 2004
EHD1 may regulate/participate in the functional pathways of both GS32 and syndapin II in a mutual exclusive manner
share on facebooktweetadd +1mail to friends