Linked Life Data

15102922

Source:http://linkedlifedata.com/resource/pubmed/id/15102922

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2004-4-22
pubmed:abstractText
Presynaptic Ca(V)2.2 (N-type) calcium channels are subject to modulation by interaction with syntaxin 1 and by a syntaxin 1-sensitive Galpha(O) G-protein pathway. We used biochemical analysis of neuronal tissue lysates and a new quantitative test of colocalization by intensity correlation analysis at the giant calyx-type presynaptic terminal of the chick ciliary ganglion to explore the association of Ca(V)2.2 with syntaxin 1 and Galpha(O). Ca(V)2.2 could be localized by immunocytochemistry (antibody Ab571) in puncta on the release site aspect of the presynaptic terminal and close to synaptic vesicle clouds. Syntaxin 1 coimmunoprecipitated with Ca(V)2.2 from chick brain and chick ciliary ganglia and was widely distributed on the presynaptic terminal membrane. A fraction of the total syntaxin 1 colocalized with the Ca(V)2.2 puncta, whereas the bulk colocalized with MUNC18-1. Galpha(O,) whether in its trimeric or monomeric state, did not coimmunoprecipitate with Ca(V)2.2, MUNC18-1, or syntaxin 1. However, the G-protein exhibited a punctate staining on the calyx membrane with an intensity that varied in synchrony with that for both Ca channels and syntaxin 1 but only weakly with MUNC18-1. Thus, syntaxin 1 appears to be a component of two separate complexes at the presynaptic terminal, a minor one at the transmitter release site with Ca(V)2.2 and Galpha(O), as well as in large clusters remote from the release site with MUNC18-1. These syntaxin 1 protein complexes may play distinct roles in presynaptic biology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4070-81
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15102922-Animals, pubmed-meshheading:15102922-Antibody Specificity, pubmed-meshheading:15102922-Antigens, Surface, pubmed-meshheading:15102922-Blotting, Western, pubmed-meshheading:15102922-Brain Chemistry, pubmed-meshheading:15102922-Calcium Channels, N-Type, pubmed-meshheading:15102922-Cells, Cultured, pubmed-meshheading:15102922-Chick Embryo, pubmed-meshheading:15102922-GTP-Binding Protein alpha Subunits, Gi-Go, pubmed-meshheading:15102922-Immunohistochemistry, pubmed-meshheading:15102922-Macromolecular Substances, pubmed-meshheading:15102922-Munc18 Proteins, pubmed-meshheading:15102922-Nerve Tissue Proteins, pubmed-meshheading:15102922-Presynaptic Terminals, pubmed-meshheading:15102922-Rats, pubmed-meshheading:15102922-Syntaxin 1, pubmed-meshheading:15102922-Vesicular Transport Proteins
pubmed:year
2004
pubmed:articleTitle
A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization.
pubmed:affiliation
Cellular and Molecular Biology Division, Toronto Western Research Institute, University Health Network, Toronto, Ontario, M5T 2S8 Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't