| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.8663905 |
| We also show that syntaxin 1A binds to and inhibits the activities of disease associated mutants of CFTR , and that the chloride current activity of recombinant DeltaF 508 CFTR ( i . e . , the most common cystic fibrosis mutant ) can be potentiated by disrupting its interaction with syntaxin 1A in cultured epithelial cells . 0.8663905^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| It was recently shown that CFTR mediated chloride currents can be regulated by syntaxin 1A , a t SNARE family member , through direct protein protein interaction . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| Syntaxin 1A inhibits regulated CFTR trafficking in xenopus oocytes . ^^^ CFTR Cl currents are regulated also by syntaxin 1A ( A . ^^^ To examine the mechanism of syntaxin 1A inhibition , we expressed these proteins in Xenopus oocytes and monitored agonist induced changes in plasma membrane capacitance and cell surface fluorescence of CFTR that contains an external epitope tag . cAMP stimulation elicited large increases in membrane capacitance and in cell surface labeling of flag tagged CFTR . ^^^ Coexpression of CFTR with syntaxin 1A , but not syntaxin 3 , inhibited cAMP induced increases in membrane capacitance and plasma membrane CFTR content . ^^^ Inhibition of plasma membrane CFTR content by syntaxin 1A is consistent with the concept that syntaxin and other components of the SNARE machinery are involved in regulated trafficking of CFTR . . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| Syntaxin 1A is expressed in airway epithelial cells , where it modulates CFTR Cl ( ) currents . ^^^ Previously , we showed that CFTR mediated Cl ( ) currents in the Xenopus oocyte expression system are inhibited by syntaxin 1A , a component of the membrane trafficking machinery . ^^^ This negative modulation of CFTR function can be reversed by soluble syntaxin 1A peptides and by the syntaxin 1A binding protein , Munc 18 . ^^^ In the present study , we determined whether syntaxin 1A is expressed in native epithelial tissues that normally express CFTR and whether it modulates CFTR currents in these tissues . ^^^ Using immunoblotting and immunofluorescence , we observed syntaxin 1A in native gut and airway epithelial tissues and showed that epithelial cells from these tissues express syntaxin 1A at > 10 fold molar excess over CFTR . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| Co expression of syntaxin 1A inhibits cAMP stimulated current and capacitance changes in CFTR expressing cells and blocks cAMP induced increases in cell surface CFTR . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| This review examines recent studies of the cystic fibrosis transmembrane conductance regulator and the epithelial sodium channel which define distinct roles of syntaxin 1A and syntaxin 3 in the regulation of surface expression as well as intrinsic properties of these epithelial ion transporters . . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| This review focuses on the regulation of ENaC by recently described accessory proteins , mainly Nedd 4 , syntaxin 1A , CFTR , sgk , K Ras2A and Cap 1 . . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| This domain directly interacted with syntaxin 1A , a SNARE protein involved in both neurotransmitter release and modulation of calcium channels and cystic fibrosis transmembrane regulator ( CFTR ) chloride channels . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| Mechanisms of CFTR regulation by syntaxin 1A and PKA . ^^^ Activation of the chloride selective anion channel CFTR is stimulated by cAMP dependent phosphorylation and is regulated by the target membrane t SNARE syntaxin 1A . ^^^ SNARE proteins play a well known role in exocytosis and have recently been implicated in the regulation of ion channels ; therefore this investigation sought to resolve two related issues : ( a ) is PKA activation or SNARE protein modulation of CFTR linked to changes in membrane turnover and ( b ) does syntaxin 1A modulate CFTR via direct effects on the gating of channels residing in the plasma membrane versus alterations in membrane traffic . ^^^ Our data demonstrate that syntaxin 1A inhibits CFTR as a result of direct protein protein interactions that decrease channel open probability ( P ( o ) ) and serves as a model for other SNARE protein ion channel interactions . ^^^ We also show that PKA activation can enhance membrane trafficking in some epithelial cell types , and this is independent from CFTR activation or syntaxin 1A association . . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| CFTR chloride channels are regulated by a SNAP 23 / syntaxin 1A complex . ^^^ Individual t SNAREs ( e . g . , syntaxin 1A ) also regulate synaptic calcium channels and cystic fibrosis transmembrane conductance regulator ( CFTR ) , the epithelial chloride channel that is defective in cystic fibrosis . ^^^ Here we show that CFTR channels are coordinately regulated by two cognate t SNAREs , SNAP 23 ( synaptosome associated protein of 23 kDa ) and syntaxin 1A . ^^^ The physical and functional interactions between SNAP 23 and CFTR depend on syntaxin 1A , which binds to both proteins . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| Syntaxin 1A binds to and inhibits epithelial cystic fibrosis transmembrane conductance regulator ( CFTR ) Cl ( ) channels and synaptic Ca ( 2+ ) channels in addition to participating in SNARE complex assembly and membrane fusion . ^^^ We exploited the isoform specific nature of the interaction between syntaxin 1A and CFTR to identify residues in the H 3 domain of this SNARE ( SNARE motif ) that influence CFTR binding and regulation . ^^^ Mutating isoform specific residues that map to the surface of syntaxin 1A in the SNARE complex led to the identification of two sets of hydrophilic residues that are important for binding to and regulating CFTR channels or for binding to the syntaxin regulatory protein Munc 18a . ^^^ Conversely , the syntaxin 1A CFTR interaction was unaffected by mutating hydrophobic residues in the H 3 domain that influence SNARE complex stability and Ca ( 2+ ) channel regulation . ^^^ Thus , CFTR channel regulation by syntaxin 1A involves hydrophilic interactions that are mechanistically distinct from the hydrophobic interactions that mediate SNARE complex formation and Ca ( 2+ ) channel regulation by this t SNARE . . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| We also demonstrated that other signaling related proteins such as Gbeta and syntaxin 1A can be in this higher order complex of CFTR as well . ^^^ |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16623 and P13569 |
Pubmed |
SVM Score :0.56715847 |
| The physical and functional interactions between syntaxin 1A and CFTR are blocked by a syntaxin binding protein of the Munc 18 protein family ( also called n Secl ) . 0.56715847^^^ |
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