Characterization of soluble N-ethylmaleimide-sensitive factor attachment protein receptor gene STX18 variations for possible roles in congenital heart diseases

Gene ◽  
2017 ◽  
Vol 598 ◽  
pp. 79-83 ◽  
Author(s):  
Xia Li ◽  
Shuai Shi ◽  
Fei-Feng Li ◽  
Rui Cheng ◽  
Ying Han ◽  
...  
Keyword(s):  
Congenital Heart ◽  
Heart Diseases ◽  
Receptor Gene ◽  
Congenital Heart Diseases ◽  
Attachment Protein ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Factor Attachment Protein Receptor

scholarly journals Characterization of VAMP isoforms in 3T3-L1 adipocytes: implications for GLUT4 trafficking

2015 ◽  
Vol 26 (3) ◽  
pp. 530-536 ◽  
Author(s):  
Jessica B. A. Sadler ◽  
Nia J. Bryant ◽  
Gwyn W. Gould
Keyword(s):  
Plasma Membrane ◽  
Snare Complex ◽  
Cell Type ◽  
Attachment Protein ◽  
Systematic Analysis ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Factor Attachment Protein Receptor

The fusion of GLUT4-containing vesicles with the plasma membrane of adipocytes is a key facet of insulin action. This process is mediated by the formation of functional soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complexes between the plasma membrane t-SNARE complex and the vesicle v-SNARE or VAMP. The t-SNARE complex consists of Syntaxin4 and SNAP23, and whereas many studies identify VAMP2 as the v-SNARE, others suggest that either VAMP3 or VAMP8 may also fulfil this role. Here we characterized the levels of expression, distribution, and association of all the VAMPs expressed in 3T3-L1 adipocytes to provide the first systematic analysis of all members of this protein family for any cell type. Despite our finding that all VAMP isoforms form SDS-resistant SNARE complexes with Syntaxin4/SNAP23 in vitro, a combination of levels of expression (which vary by >30-fold), subcellular distribution, and coimmunoprecipitation analyses lead us to propose that VAMP2 is the major v-SNARE involved in GLUT4 trafficking to the surface of 3T3-L1 adipocytes.

scholarly journals A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion

2008 ◽  
Vol 19 (8) ◽  
pp. 3379-3389 ◽  
Author(s):  
Elena Fdez ◽  
Thomas A. Jowitt ◽  
Ming-Chuan Wang ◽  
Manisha Rajebhosale ◽  
Keith Foster ◽  
...  
Keyword(s):  
Dominant Negative ◽  
Neuroendocrine Cells ◽  
Snare Complex ◽  
Membrane Interface ◽  
Attachment Protein ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
The Stability ◽  
Factor Attachment Protein Receptor

The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE complexes are in apposition, and it involves residues from the vesicle-associated SNARE synaptobrevin 2 that lie close to the cytosol–membrane interface within the full-length protein. Mutation of these residues reduces stability of dimers formed between SNARE complexes, without affecting the stability of each individual SNARE complex. These mutations also cause a corresponding decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells. Moreover, such synaptobrevin 2 mutants give rise to a dominant-negative inhibition of exocytosis. These data are consistent with an important role for SNARE complex dimers in neurosecretion.

scholarly journals Characterization of SMAD3 Gene Variants for Possible Roles in Ventricular Septal Defects and Other Congenital Heart Diseases

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0131542 ◽  
Author(s):  
Fei-Feng Li ◽  
Jing Zhou ◽  
Dan-Dan Zhao ◽  
Peng Yan ◽  
Xia Li ◽  
...  
Keyword(s):  
Congenital Heart ◽  
Heart Diseases ◽  
Congenital Heart Diseases ◽  
Gene Variants ◽  
Ventricular Septal Defects ◽  
Septal Defects

scholarly journals Syntaxin 16 is a master recruitment factor for cytokinesis

2013 ◽  
Vol 24 (23) ◽  
pp. 3663-3674 ◽  
Author(s):  
Hélia Neto ◽  
Alexandra Kaupisch ◽  
Louise L. Collins ◽  
Gwyn W. Gould
Keyword(s):  
Membrane Vesicles ◽  
Attachment Protein ◽  
Recycling Endosome ◽  
Endosomal Sorting ◽  
Escrt Machinery ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Late Telophase ◽  
Intracellular Organelles ◽  
Factor Attachment Protein Receptor

Recently it was shown that both recycling endosome and endosomal sorting complex required for transport (ESCRT) components are required for cytokinesis, in which they are believed to act in a sequential manner to bring about secondary ingression and abscission, respectively. However, it is not clear how either of these complexes is targeted to the midbody and whether their delivery is coordinated. The trafficking of membrane vesicles between different intracellular organelles involves the formation of soluble N-ethylmalei­mide–sensitive factor attachment protein receptor (SNARE) complexes. Although membrane traffic is known to play an important role in cytokinesis, the contribution and identity of intracellular SNAREs to cytokinesis remain unclear. Here we demonstrate that syntaxin 16 is a key regulator of cytokinesis, as it is required for recruitment of both recycling endosome–associated Exocyst and ESCRT machinery during late telophase, and therefore that these two distinct facets of cytokinesis are inextricably linked.

scholarly journals Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane

2011 ◽  
Vol 22 (21) ◽  
pp. 4134-4149 ◽  
Author(s):  
Gayoung A. Han ◽  
Nancy T. Malintan ◽  
Ner Mu Nar Saw ◽  
Lijun Li ◽  
Liping Han ◽  
...  
Keyword(s):  
Molecular Chaperone ◽  
Dense Core ◽  
Dense Core Vesicle ◽  
Attachment Protein ◽  
Vesicle Docking ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Intracellular Expression ◽  
Factor Attachment Protein Receptor

Munc18-1 plays pleiotropic roles in neurosecretion by acting as 1) a molecular chaperone of syntaxin-1, 2) a mediator of dense-core vesicle docking, and 3) a priming factor for soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion. However, how these functions are executed and whether they are correlated remains unclear. Here we analyzed the role of the domain-1 cleft of Munc18-1 by measuring the abilities of various mutants (D34N, D34N/M38V, K46E, E59K, K46E/E59K, K63E, and E66A) to bind and chaperone syntaxin-1 and to restore the docking and secretion of dense-core vesicles in Munc18-1/-2 double-knockdown cells. We identified striking correlations between the abilities of these mutants to bind and chaperone syntaxin-1 with their ability to restore vesicle docking and secretion. These results suggest that the domain-1 cleft of Munc18-1 is essential for binding to syntaxin-1 and thereby critical for its chaperoning, docking, and secretory functions. Our results demonstrate that the effect of the alleged priming mutants (E59K, D34N/M38V) on exocytosis can largely be explained by their reduced syntaxin-1–chaperoning functions. Finally, our data suggest that the intracellular expression and distribution of syntaxin-1 determines the level of dense-core vesicle docking.

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