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These observations suggest an important role for SNAPIN and autophagy in the homeostasis of macrophages, particularly long-lived tissue resident macrophages.
These results provide the evidence of a direct regulatory role of Snapin on Cav1.3 (show CACNA1D Proteins) channels in atrial myocytes.
Inhibition of Snapin enhanced localization of HIV-1 with TLR8 (show TLR8 Proteins)(+) early endosomes, triggered a pro-inflammatory response, and inhibited trans-infection of CD4 (show CD4 Proteins)(+) T cells.
Taken together, these results suggest that Snapin, the pUL130 interacting protein, has a role in modulating HCMV DNA synthesis.
Disruption of Snapin-PKR2 (show PROKR2 Proteins) interaction did not affect PKR2 (show PROKR2 Proteins) signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2 (show PROKR2 Proteins).
Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein.
Snapin, a SNAP (show NAPA Proteins)-25 (synaptosomal-associated protein-25 (show SNAP25 Proteins)) interacting protein, interacts with LRRK2.
Our findings reveal that Atg14L, previously considered to be solely a Beclin 1 (show BECN1 Proteins)-binding autophagy protein, plays a novel role in the late stage of endocytic trafficking in conjunction with Snapin
These observations identify Snapin as a novel endogenous TLR2 ligand in rheumatoid arthritis, and thus support a role for persistent TLR2 signalling in pathogenesis.
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-dysbindin interaction regulates synaptic vesicle positional priming through BLOC-1/AP-3-dependent sorting.
Snapin reduces APP (show APP Proteins) processing by enhancing BACE1 (show BACE Proteins) lysosomal degradation.
Transmembrane prostatic acid phosphatase (show ACPP Proteins) (TMPAP) interacts with snapin and deficient mice develop prostate adenocarcinoma.
Snapin accelerates exocytosis at low intracellular calcium concentration in mouse chromaffin cells.
Snapin-dynein coupling is one of the primary mechanisms driving BDNF (show BDNF Proteins)-TrkB (show NTRK2 Proteins) retrograde transport, thus providing mechanistic insights into the regulation of neuronal growth and survival.
AC6 (show ADCY6 Proteins)-mediated inhibition of neurite outgrowth was reversed by the overexpression of Snap25 (show SNAP25 Proteins) or a Snapin mutant that could not be phosphorylated.
Snapin has a role in regulating autophagy-lysosomal function
PKA-dependent phosphorylation of snapin increases interaction among insulin (show INS Proteins) secretory vesicle-associated proteins, thereby potentiating glucose-stimulated insulin (show INS Proteins) secretion.
Snapin deficiency leads to reduced cell density in cortical plates, apoptotic death in the cortex & third ventricle, enhanced membrane-bound LC3 (show MAP1LC3A Proteins)-II staining, and accumulation of polyubiquitinated proteins in the cortex and hippocampus in knockout mice
The protein encoded by this gene is a coiled-coil-forming protein that associates with the SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complex of proteins and the BLOC-1 (biogenesis of lysosome-related organelles) complex. Biochemical studies have identified additional binding partners. As part of the SNARE complex, it is required for vesicle docking and fusion and regulates neurotransmitter release. The BLOC-1 complex is required for the biogenesis of specialized organelles such as melanosomes and platelet dense granules. Mutations in gene products that form the BLOC-1 complex have been identified in mouse strains that are models of Hermansky-Pudlak syndrome. Alternative splicing results in multiple transcript variants.
, SNARE-associated protein Snapin
, BLOC-1 subunit 7
, SNAP-25-binding protein
, SNARE associated protein snapin
, biogenesis of lysosomal organelles complex-1, subunit 7
, biogenesis of lysosome-related organelles complex 1 subunit 7
, synaptosomal-associated protein 25-binding protein
, synaptosomal-associated protein 25 binding protein
, synaptosomal-associated protein, 25 kDa, binding protein