Linked Life Data

12482583

Source:http://linkedlifedata.com/resource/pubmed/id/12482583

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-12-16
pubmed:abstractText
We characterized the neuronal two-domain (95kD-alpha(1)2.1) form of the alpha(1)2.1 subunit of the voltage-gated calcium channels using genetic and molecular analysis. The 95kD-alpha(1)2.1 is absent in neuronal preparations from CACNA1A null mouse demonstrating that alpha(1)2.1 and 95kD-alpha(1)2.1 arise from the same gene. A recombinant two-domain form (alpha(1AI-II)) of alpha(1)2.1 associates with the beta subunit and is trafficked to the plasma membrane. Translocation of the alpha(1AI-II) to the plasma membrane requires association with the beta subunit, since a mutation in the alpha(1AI-II) that inhibits beta subunit association reduces membrane trafficking. Though the alpha(1AI-II) protein does not conduct any voltage-gated currents, we have previously shown that it generates a high density of non-linear charge movements [Ahern et al., Proc. Natl. Acad. Sci. USA 98 (2001) 6935-6940]. In this study, we demonstrate that co-expression of the alpha(1AI-II) significantly reduces the current amplitude of alpha(1)2.1/beta(1a)/alpha(2)delta channels, via competition for the beta subunit. Taken together, our results demonstrate a dual functional role for the alpha(1AI-II) protein, both as a voltage sensor and modulator of P/Q-type currents in recombinant systems. These studies suggest an in vivo role for the 95kD-alpha(1)2.1 in altering synaptic activity via protein-protein interactions and/or regulation of P/Q-type currents.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
532
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
300-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12482583-Animals, pubmed-meshheading:12482583-Brain, pubmed-meshheading:12482583-Calcium Channels, pubmed-meshheading:12482583-Calcium Channels, P-Type, pubmed-meshheading:12482583-Calcium Channels, Q-Type, pubmed-meshheading:12482583-Cell Line, pubmed-meshheading:12482583-Cell Nucleus, pubmed-meshheading:12482583-Cells, Cultured, pubmed-meshheading:12482583-Cerebellum, pubmed-meshheading:12482583-Cricetinae, pubmed-meshheading:12482583-DNA, Complementary, pubmed-meshheading:12482583-Electrophysiology, pubmed-meshheading:12482583-Green Fluorescent Proteins, pubmed-meshheading:12482583-Luminescent Proteins, pubmed-meshheading:12482583-Microscopy, Confocal, pubmed-meshheading:12482583-Neurons, pubmed-meshheading:12482583-Precipitin Tests, pubmed-meshheading:12482583-Protein Binding, pubmed-meshheading:12482583-Protein Structure, Tertiary, pubmed-meshheading:12482583-Rabbits, pubmed-meshheading:12482583-Recombinant Proteins, pubmed-meshheading:12482583-Transfection
pubmed:year
2002
pubmed:articleTitle
Molecular characterization of a two-domain form of the neuronal voltage-gated P/Q-type calcium channel alpha(1)2.1 subunit.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Physiology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242-1101, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't