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data implicates beta1 integrin, FAK (show PTK2 Proteins), and paxillin (show PXN Proteins) in mediating the observed pro-adhesive effects of alphaSNAP. These results reveal novel roles for alphaSNAP in regulating ECM (show MMRN1 Proteins) adhesion and motility of epithelial cells.
Study revealed a novel role for alphaSNAP as a negative regulator of autophagy that acts by enhancing mTOR (show FRAP1 Proteins) signaling and regulating the integrity of the Golgi complex.
The most N-terminal part of BKV agnoprotein is involved in the interaction with alpha-SNAP
a novel role for alphaSNAP in promoting epithelial cell survival by unique mechanisms involving regulation of Bcl-2 (show BCL2 Proteins) expression and Golgi biogenesis
Results suggest that the combinational SNARE proteins VAMP8 and Vti1b mediate the fusion of antimicrobial and canonical autophagosomes with lysosomes, an essential event for autophagic degradation.
alpha-SNAP plays a key role in the acrosome reaction.
G alpha12 interaction with alphaSNAP induces VE-cadherin (show CDH5 Proteins) localization at endothelial junctions and regulates barrier function
alpha-SNAP destabilized the linker domain (LD) of the SNARE complex but stabilized its C-terminal domain.
alpha-SNAP is a crucial component of Orai1 (show TMEM132A Proteins) channels, and its depletion disrupts the functional assembly of Orai1 (show TMEM132A Proteins) multimers. Here the authors show that alpha-SNAP hypomorph, hydrocephalus with hopping gait, Napa(hyh/hyh) mice harbor significant defects in CD4 (show CD4 Proteins) T cell gene expression and Foxp3 (show FOXP3 Proteins) regulatory T cell (Treg) differentiation.
Furthermore, alphaSNAP-deficient mutant animals displayed reduced formation of lysozyme granules in small intestinal crypts and decreased expression of lysozyme and defensins in the intestinal mucosa, which is indicative of defects in Paneth cell differentiation. By contrast, development of Goblet cells, enteroendocrine cells, and assembly of enterocyte apical junctions was not altered in hyh mutant mice. Our data reve...
AMPK (show PRKAA1 Proteins) associates with alpha-SNAP, an adapter that enables disassembly of cis (show CISH Proteins)-SNARE (show VTI1B Proteins) complexes formed during membrane fusion.
analysis of alpha- and betaSNAP deletion mutant neurons shows that the two N-Ethylmaleimide-Sensitive Factor (show NSF Proteins) cofactors support synaptic vesicle priming by determining the availability of free SNARE (show VTI1B Proteins) components
Study indicate that the genotyping method enhances the potentiality of hyh mouse as a unique in vivo model to study the role of membrane trafficking in different developmental and physiological processes.
The hyh mutation uncovers roles for alpha Snap in apical protein localization and control of neural cell fate.
This gene encodes a member of the soluble NSF attachment protein (SNAP) family. SNAP proteins play a critical role in the docking and fusion of vesicles to target membranes as part of the 20S NSF-SNAP-SNARE complex. The encoded protein plays a role in the completion of membrane fusion by mediating the interaction of N-ethylmaleimide-sensitive factor (NSF) with the vesicle-associated and membrane-associated SNAP receptor (SNARE) complex, and stimulating the ATPase activity of NSF. Alternatively spliced transcript variants have been observed for this gene.
, alpha-soluble NSF attachment protein
, N-ethylmaleimide-sensitive factor attachment protein, beta
, N-ethylmaleimide sensitive fusion protein attachment protein alpha
, N-ethylmaleimide-sensitive factor attachment protein alpha
, N-ethylmaleimide-sensitive factor attachment protein, alpha
, hydrocephaly with hop gait