Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-2-1
pubmed:abstractText
In neuronal and hormonal release, regulated exocytosis requires an essential set of proteins: the soluble N-ethylmaleimide sensitive-factor attachment receptor proteins (SNAREs) syntaxin 1, SNAP-25, VAMP, and their regulator, Munc18. Recently, it was found that Munc18-1 can interact with syntaxin 1 through distinct mechanisms: an inhibitory mode enveloping syntaxin (mode 1), sequestering it from SNARE protein interactions, and direct binding to an evolutionarily conserved N-terminal peptide of syntaxin (mode 2/3). The latter interaction has been proposed to control "priming" of the fusion reaction, defined using electrophysiology, but it is unknown how this interaction is regulated, and any dynamic effect at the molecular or vesicular level in cells remains undiscovered. We now show that a phosphorylation site in syntaxin 1 (Ser(14)) regulates the N-terminal interaction with Munc18-1. Probing syntaxin 1 association with Munc18-1, in real-time and in living cells, we found that modification of Ser(14) modulated the dynamics of this interaction, specifically at the plasma membrane. Destabilization of this dynamic interaction enhanced vesicle immobilization at the plasma membrane with a resulting inhibition of exocytosis.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-10648557, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-10746715, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-10844023, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-10893260, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-11545717, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-11832947, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-12154365, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-12426383, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-12519779, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-12667755, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-12676086, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-15230870, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-15489225, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-15911375, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-16537489, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-16769821, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-16899085, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-16912714, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17090679, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17205130, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17218264, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17264080, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17287513, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17301226, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17363971, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17407758, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17517664, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17551585, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17893335, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-17906638, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-18003982, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-18057031, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-18077557, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-18337752, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-19255244, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-19295602, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-2371284, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-3464423, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-8060616, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-8221884, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-8463845, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-8631738, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-9529252, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-9759724, http://linkedlifedata.com/resource/pubmed/commentcorrection/19748891-9930733
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3965-72
pubmed:dateRevised
2010-9-28
pubmed:meshHeading
pubmed-meshheading:19748891-Amino Acid Sequence, pubmed-meshheading:19748891-Animals, pubmed-meshheading:19748891-Casein Kinase II, pubmed-meshheading:19748891-Cell Line, Tumor, pubmed-meshheading:19748891-Cell Membrane, pubmed-meshheading:19748891-Exocytosis, pubmed-meshheading:19748891-Kinetics, pubmed-meshheading:19748891-Luminescent Proteins, pubmed-meshheading:19748891-Microscopy, Confocal, pubmed-meshheading:19748891-Molecular Sequence Data, pubmed-meshheading:19748891-Munc18 Proteins, pubmed-meshheading:19748891-PC12 Cells, pubmed-meshheading:19748891-Phosphorylation, pubmed-meshheading:19748891-Protein Binding, pubmed-meshheading:19748891-Rats, pubmed-meshheading:19748891-Secretory Vesicles, pubmed-meshheading:19748891-Sequence Homology, Amino Acid, pubmed-meshheading:19748891-Serine, pubmed-meshheading:19748891-Syntaxin 1, pubmed-meshheading:19748891-Transfection
pubmed:year
2010
pubmed:articleTitle
Munc18/Syntaxin interaction kinetics control secretory vesicle dynamics.
pubmed:affiliation
Centre for Integrative Physiology, University of Edinburgh, George Square, Edinburgh EH8 9XD, Scotland, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't