Role of SNAP-23 in trafficking of H+-ATPase in cultured inner medullary collecting duct cells.

@article{Banerjee2001RoleOS,
  title={Role of SNAP-23 in trafficking of H+-ATPase in cultured inner medullary collecting duct cells.},
  author={Ayan Banerjee and G Li and Edward A. Alexander and John H. Schwartz},
  journal={American journal of physiology. Cell physiology},
  year={2001},
  volume={280 4},
  pages={
          C775-81
        }
}
The trafficking of H+-ATPase vesicles to the apical membrane of inner medullary collecting duct (IMCD) cells utilizes a mechanism similar to that described in neurosecretory cells involving soluble N-ethylmaleimide-sensitive factor attachment protein target receptor (SNARE) proteins. Regulated exocytosis of these vesicles is associated with the formation of SNARE complexes. Clostridial neurotoxins that specifically cleave the target (t-) SNARE, syntaxin-1, or the vesicle SNARE, vesicle… 
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Role of SNAREs and H+-ATPase in the targeting of proton pump-coated vesicles to collecting duct cell apical membrane.

It is found that Munc-18-2, a regulator of exocytosis, plays a multifunctional role in this system: it regulates SNARE complex formation and the affinity of syntaxin 1 for H(+)-ATPase.

Syntaxin Isoform Specificity in the Regulation of Renal H+-ATPase Exocytosis*

This work has shown that the exocytic insertion of proton pumps into the apical membrane of rat IMCD cells, in culture, involves SNARE proteins (syntaxin (synt), SNAP-23, and VAMP), and suggested that the targeting of these vesicles to the apicals membrane is mediated by an interaction between the H+-ATPase and a specific t-SNARE.

Munc-18-2 regulates exocytosis of H(+)-ATPase in rat inner medullary collecting duct cells.

It is concluded that Munc-18-2 must dissociate from the syntaxin 1A protein for the exocytosis of H(+)-ATPase to occur and this dissociation leads to a conformational change in syntaxin1A, allowing it to interact with H( +)-ATTPase, synaptosome-associated protein (SNAP)-23, and vesicle-associated membrane protein (VAMP), forming the SNARE complex that leads to

Collectrin Is Involved in the Development of Salt-Sensitive Hypertension by Facilitating the Membrane Trafficking of Apical Membrane Proteins via Interaction With Soluble N-Ethylmaleiamide–Sensitive Factor Attachment Protein Receptor Complex

Upregulation of collectrin by high NaCl independent of aldosterone functionally links to the trafficking of apical membrane proteins via the SNARE complex, and collectrin may be responsible for the sodium retention in salt-sensitive hypertension.

Syntaxin 1A has a specific binding site in the H3 domain that is critical for targeting of H+-ATPase to apical membrane of renal epithelial cells.

It is concluded that within the H3 domain of syntaxin 1A is a unique cassette that participates in the binding of the H(+)-ATPase to the apical membrane and confers specificity of syntax in 1A in the process of H( +)- ATPase exocytosis.

Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Results represent the first evidence for the functional involvement of VAMP-2 in cAMP-induced AQP2 exocytosis in renal cells.

Identification of SNAREs Involved in Synaptotagmin VII-regulated Lysosomal Exocytosis*

Lysosomal exocytosis was inhibited by the SNARE domains of syntaxin 4 and TI-VAMP/VAMP7 and by cleavage of SNAP-23 with botulinum neurotoxin E, thereby functionally implicating these SNAREs in Ca2+-regulated exocyTosis of conventional lysosomes.

A dominant-negative variant of SNAP-23 decreases the cell surface expression of the neuronal glutamate transporter EAAC1 by slowing constitutive delivery

New insights into the regulation of V-ATPase-dependent proton secretion.

The vacuolar H(+)-ATPase (V-ATPase) is a key player in several aspects of cellular function, including acidification of intracellular organelles and regulation of extracellular pH. In specialized…

Syntaxin 3 is necessary for cAMP- and cGMP-regulated exocytosis of CFTR: implications for enterotoxigenic diarrhea.

A new and important role is revealed for syntaxin 3 in the pathophysiology of enterotoxin-elicited diarrhea by identifying components of the exocytic soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) vesicle fusion machinery in cyclic nucleotide-activated exocytosis of CFTR in rat jejunum and polarized intestinal Caco-2(BB)e cells.

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