Localization and Function of SolubleN-Ethylmaleimide-sensitive Factor Attachment Protein-25 and Vesicle-associated Membrane Protein-2 in Functioning Gastric Parietal Cells

Karvar, Serhan; Yao, Xuebiao; Crothers, James M.; Liu, Yuechueng; Forte, John G.

doi:10.1074/jbc.m207694200

Cited by 35 publications

(21 citation statements)

References 35 publications

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“…These data are consistent with the observation that the expression of these molecules is more restricted to neuronal and neuroendocrine tissues (38 -40). However, the presence of Syntaxin-1 and VAMP-1 has been documented in other non-neuronal cells as neutrophils and osteoblasts (41)(42)(43), and the expression of SNAP-25 has been demonstrated in gastric parietal cells and eosinophils (44,45). The RT-PCR results presented here in normal PC, but not in PC lines (Fig.…”

Section: Discussionmentioning

confidence: 64%

Identification of Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Exocytotic Machinery in Human Plasma Cells: SNAP-23 Is Essential for Antibody Secretion

Reales

Mora-López

Rivas

et al. 2005

The Journal of Immunology

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Plasma cells (PC) are B-lymphocytes terminally differentiated in a postmitotic state, with the unique purpose of manufacturing and exporting Igs. Despite the importance of this process in the survival of vertebrates, no studies have been made to understand the molecular events that regulate Ig exocytosis by PC. The present study explores the possible presence of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) system in human PC, and examines its functional role in Ig secretion. Syntaxin-2, Syntaxin-3, Syntaxin-4, vesicle-associated membrane protein (VAMP)-2, VAMP-3, and synaptosome-associated protein (SNAP)-23 could be readily detected in normal human PC obtained from intestinal lamina propria and blood, as well as in human PC lines. Because SNAP-23 plays a central role in SNAREs complex formation, it was chosen to examine possible functional implications of the SNARE system in PC Ig secretion. When recombinant SNAP-23 fusion protein was introduced into the cells, a complete abolishment of Ig production was observed in the culture supernatants of PC lines, as well as in those of normal PC. These results provide insights, for the first time, into the molecular machinery of constitutive vesicular trafficking in human PC Ig secretion and present evidence indicating that at least SNAP-23 is essential for Ab production.

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Section: Discussionmentioning

confidence: 64%

Identification of Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Exocytotic Machinery in Human Plasma Cells: SNAP-23 Is Essential for Antibody Secretion

Reales

Mora-López

Rivas

et al. 2005

The Journal of Immunology

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“…The SNARE core complex components must be delivered to the membranes by trafficking machinery, and failure to target these proteins disrupts vesicular trafficking in polarized cells (Reales et al, 2011). In parietal cells, fusion of recycling tubulovesicles to the apical surface is mediated by the syntaxin 3 (STX3), VAMP2 and SNAP25 core SNARE complex (Calhoun et al, 1998;Karvar et al, 2002). STX3 appears to play a general role in targeting of vesicle fusion events at the apical membranes in epithelial cells.…”

Section: Introductionmentioning

confidence: 99%

Rab11a regulates Syntaxin 3 localization and microvillus assembly in enterocytes

Knowles

Weis

et al. 2015

Journal of Cell Science

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Rab11a is a key component of the apical recycling endosome that aids in the trafficking of proteins to the luminal surface in polarized epithelial cells. Utilizing conditional Rab11a-knockout specific to intestinal epithelial cells, and human colonic epithelial CaCo2-BBE cells with stable Rab11a knockdown, we examined the molecular and pathological impact of Rab11a deficiency on the establishment of apical cell polarity and microvillus morphogenesis. We demonstrate that loss of Rab11a induced alterations in enterocyte polarity, shortened microvillar length and affected the formation of microvilli along the lateral membranes. Rab11a deficiency in enterocytes altered the apical localization of syntaxin 3. These data affirm the role of Rab11a in apical membrane trafficking and the maintenance of apical microvilli in enterocytes.

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“…The three SNARE proteins form a four-helical bundle, the SNARE complex, which mediates membrane fusion (9). Our recent studies demonstrate the functional significance of Stx3 (10), VAMP2 (11), and SNAP25 (12) in the parietal cell exocytosis. Despite demonstration of the functional importance of Stx3 in parietal cell secretion (13,14), it is still unclear how Stx3 facilitates the docking tubulovesicular membrane at the apical membrane.…”

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confidence: 99%

Spatial Control of Proton Pump H,K-ATPase Docking at the Apical Membrane by Phosphorylation-coupled Ezrin-Syntaxin 3 Interaction

Zhang

Takahashi

et al. 2014

Journal of Biological Chemistry

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Background: Polarized acid secretion in gastric parietal cells requires ezrin and its phosphorylation at Ser-66. Results: Phosphorylation of Ser-66 induces ezrin conformational change, which enables ezrin to interact with syntaxin 3. Conclusion: Conformational change of ezrin provides a spatial cue for apical trafficking of H,K-ATPase. Significance: Ezrin conformation orchestrates the polarized vesicle trafficking in epithelial cells.

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Localization and Function of SolubleN-Ethylmaleimide-sensitive Factor Attachment Protein-25 and Vesicle-associated Membrane Protein-2 in Functioning Gastric Parietal Cells

Cited by 35 publications

References 35 publications

Identification of Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Exocytotic Machinery in Human Plasma Cells: SNAP-23 Is Essential for Antibody Secretion

Identification of Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor Exocytotic Machinery in Human Plasma Cells: SNAP-23 Is Essential for Antibody Secretion

Rab11a regulates Syntaxin 3 localization and microvillus assembly in enterocytes

Spatial Control of Proton Pump H,K-ATPase Docking at the Apical Membrane by Phosphorylation-coupled Ezrin-Syntaxin 3 Interaction

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