| http://purl.uniprot.org/citations/15489225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15489225 | http://www.w3.org/2000/01/rdf-schema#comment | "Syntaxin1A, a neural-specific N-ethylmaleimide-sensitive factor attachment protein receptor protein essential to neurotransmitter release, in isolation forms a closed conformation with an N-terminal alpha-helix bundle folded upon the SNARE motif (H3 domain), thereby limiting interaction of the H3 domain with cognate SNAREs. Munc18-1, a neural-specific member of the Sec1/Munc18 protein family, binds to syntaxin1A, stabilizing this closed conformation. We used fluorescence resonance energy transfer (FRET) to characterize the Munc18-1/syntaxin1A interaction in intact cells. Enhanced cyan fluorescent protein-Munc18-1 and a citrine variant of enhanced yellow fluorescent protein-syntaxin1A, or mutants of these proteins, were expressed as donor and acceptor pairs in human embryonic kidney HEK293-S3 and adrenal chromaffin cells. Apparent FRET efficiency was measured using two independent approaches with complementary results that unambiguously verified FRET and provided a spatial map of FRET efficiency. In addition, enhanced cyan fluorescent protein-Munc18-1 and a citrine variant of enhanced yellow fluorescent protein-syntaxin1A colocalized with a Golgi marker and exhibited FRET at early expression times, whereas a strong plasma membrane colocalization, with similar FRET values, was apparent at later times. Trafficking of syntaxin1A to the plasma membrane was dependent on the presence of Munc18-1. Both syntaxin1A(L165A/E166A), a constitutively open conformation mutant, and syntaxin1A(I233A), an H3 domain point mutant, demonstrated apparent FRET efficiency that was reduced approximately 70% from control. In contrast, the H3 domain mutant syntaxin1A(I209A) had no effect. By using phosphomimetic mutants of Munc18-1, we also established that Ser-313, a Munc18-1 protein kinase C phosphorylation site, and Thr-574, a cyclin-dependent kinase 5 phosphorylation site, regulate Munc18-1/syntaxin1A interaction in HEK293-S3 and chromaffin cells. We conclude that FRET imaging in living cells may allow correlated regulation of Munc18-1/syntaxin1A interactions to Ca(2+)-regulated secretory events."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m410024200"xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Ho C.S."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Li Q."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Lee Y.Y."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Lentz S.I."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Ernst S.A."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Stuenkel E.L."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/author | "Gladycheva S.E."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/pages | "55924-55936"xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/title | "Fluorescence resonance energy transfer reports properties of syntaxin1a interaction with Munc18-1 in vivo."xsd:string |
| http://purl.uniprot.org/citations/15489225 | http://purl.uniprot.org/core/volume | "279"xsd:string |
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