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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-10-10
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pubmed:abstractText |
We have identified a novel interaction between huntingtin (htt) and N-type calcium channels, a channel key in coupling calcium influx with synaptic vesicle exocytosis. Htt is a widely expressed 350-kDa cytosolic protein bearing an N-terminal polyglutamine tract. Htt is proteolytically cleaved by calpains and caspases and the resultant htt N-terminal fragments have been proposed to be biologically active; however, the cellular function of htt and/or the htt fragments remains enigmatic. We show that N-terminal fragments of htt (consisting of exon1) and full-length htt associate with the synaptic protein interaction (synprint) region of the N-type calcium channel. Given that synprint has previously been shown to bind syntaxin 1A and that this association elicits inhibition of N-type calcium channels, we tested whether htt(exon1) affects the modulation of these channels. Our data indicate that htt(exon1) enhances calcium influx by blocking syntaxin 1A inhibition of N-type calcium channels and attributes a key role for htt N-terminal fragments in the fine tuning of neurotransmission.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1044-7431
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
339-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16162412-Animals,
pubmed-meshheading:16162412-Animals, Newborn,
pubmed-meshheading:16162412-Calcium Channels, N-Type,
pubmed-meshheading:16162412-Calcium Signaling,
pubmed-meshheading:16162412-Cell Line,
pubmed-meshheading:16162412-Cell Membrane,
pubmed-meshheading:16162412-Exons,
pubmed-meshheading:16162412-Hippocampus,
pubmed-meshheading:16162412-Humans,
pubmed-meshheading:16162412-Mice,
pubmed-meshheading:16162412-Nerve Tissue Proteins,
pubmed-meshheading:16162412-Neuroglia,
pubmed-meshheading:16162412-Neurons,
pubmed-meshheading:16162412-Nuclear Proteins,
pubmed-meshheading:16162412-Peptide Fragments,
pubmed-meshheading:16162412-Protein Structure, Tertiary,
pubmed-meshheading:16162412-Rats,
pubmed-meshheading:16162412-Synaptic Membranes,
pubmed-meshheading:16162412-Synaptic Transmission,
pubmed-meshheading:16162412-Syntaxin 1
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pubmed:year |
2005
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pubmed:articleTitle |
Crosstalk between huntingtin and syntaxin 1A regulates N-type calcium channels.
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pubmed:affiliation |
Department of Physiology and Biophysics, Hotchkiss Brain Institute, The University of Calgary, Calgary, Alberta, Canada T2N 4N1.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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