Linked Life Data

9412493

Source:http://linkedlifedata.com/resource/pubmed/id/9412493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-1-16
pubmed:abstractText
Syntrophins are cytoplasmic peripheral membrane proteins of the dystrophin-associated protein complex (DAPC). Three syntrophin isoforms, alpha1, beta1, and beta2, are encoded by distinct genes. Each contains two pleckstrin homology (PH) domains, a syntrophin-unique (SU) domain, and a PDZ domain. The name PDZ comes from the first three proteins found to contain repeats of this domain (PSD-95, Drosophila discs large protein, and the zona occludens protein 1). PDZ domains in other proteins bind to the C termini of ion channels and neurotransmitter receptors containing the consensus sequence (S/T)XV-COOH and mediate the clustering or synaptic localization of these proteins. Two voltage-gated sodium channels (NaChs), SkM1 and SkM2, of skeletal and cardiac muscle, respectively, have this consensus sequence. Because NaChs are sarcolemmal components like syntrophins, we have investigated possible interactions between these proteins. NaChs copurify with syntrophin and dystrophin from extracts of skeletal and cardiac muscle. Peptides corresponding to the C-terminal 10 amino acids of SkM1 and SkM2 are sufficient to bind detergent-solubilized muscle syntrophins, to inhibit the binding of native NaChs to syntrophin PDZ domain fusion proteins, and to bind specifically to PDZ domains from alpha1-, beta1-, and beta2-syntrophin. These peptides also inhibit binding of the syntrophin PDZ domain to the PDZ domain of neuronal nitric oxide synthase, an interaction that is not mediated by C-terminal sequences. Brain NaChs, which lack the (S/T)XV consensus sequence, also copurify with syntrophin and dystrophin, an interaction that does not appear to be mediated by the PDZ domain of syntrophin. Collectively, our data suggest that syntrophins link NaChs to the actin cytoskeleton and the extracellular matrix via dystrophin and the DAPC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0270-6474
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
128-37
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9412493-Amino Acid Sequence, pubmed-meshheading:9412493-Animals, pubmed-meshheading:9412493-Brain Chemistry, pubmed-meshheading:9412493-Calcium-Binding Proteins, pubmed-meshheading:9412493-Cytoskeleton, pubmed-meshheading:9412493-Detergents, pubmed-meshheading:9412493-Dystrophin, pubmed-meshheading:9412493-Dystrophin-Associated Proteins, pubmed-meshheading:9412493-Extracellular Matrix, pubmed-meshheading:9412493-Membrane Proteins, pubmed-meshheading:9412493-Mice, pubmed-meshheading:9412493-Molecular Sequence Data, pubmed-meshheading:9412493-Muscle, Skeletal, pubmed-meshheading:9412493-Muscle Proteins, pubmed-meshheading:9412493-Neuromuscular Junction, pubmed-meshheading:9412493-Nitric Oxide Synthase, pubmed-meshheading:9412493-Potassium Channels, pubmed-meshheading:9412493-Protein Binding, pubmed-meshheading:9412493-Protein Structure, Tertiary, pubmed-meshheading:9412493-Sodium Channels
pubmed:year
1998
pubmed:articleTitle
Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins.
pubmed:affiliation
Department of Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7545, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't