Linked Life Data

10506186

Source:http://linkedlifedata.com/resource/pubmed/id/10506186

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1999-11-9
pubmed:databankReference
pubmed:abstractText
Here we describe the isolation and partial characterization of a new muscle-specific protein (Melusin) which interacts with the integrin cytoplasmic domain. The cDNA encoding Melusin was isolated in a two-hybrid screening of a rat neonatal heart library using beta(1)A and beta(1)D integrin cytoplasmic regions as baits. Melusin is a cysteine-rich cytoplasmic protein of 38 kDa, with a stretch of acidic amino acid residues at the extreme carboxyl-terminal end. In addition, putative binding sites for SH3 and SH2 domains are present in the amino-terminal half of the molecule. Chromosomic analysis showed that melusin gene maps at Xq12.1/13 in man and in the synthenic region X band D in mouse. Melusin is expressed in skeletal and cardiac muscles but not in smooth muscles or other tissues. Immunofluorescence analysis showed that Melusin is present in a costamere-like pattern consisting of two rows flanking alpha-actinin at Z line. Its expression is up-regulated during in vitro differentiation of the C2C12 murine myogenic cell line, and it is regulated during in vivo skeletal muscle development. A fragment corresponding to the tail region of Melusin interacted strongly and specifically with beta(1) integrin cytoplasmic domain in a two-hybrid test, but the full-length protein did not. Because the tail region of Melusin contains an acidic amino acid stretch resembling high capacity and low affinity calcium binding domains, we tested the possibility that Ca(2+) regulates Melusin-integrin association. In vitro binding experiments demonstrated that interaction of full-length Melusin with detergent-solubilized integrin heterodimers occurred only in absence of cations, suggesting that it can be regulated by intracellular signals affecting Ca(2+) concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29282-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10506186-Amino Acid Sequence, pubmed-meshheading:10506186-Animals, pubmed-meshheading:10506186-Animals, Newborn, pubmed-meshheading:10506186-Antigens, CD29, pubmed-meshheading:10506186-Calcium, pubmed-meshheading:10506186-Carrier Proteins, pubmed-meshheading:10506186-Cell Line, pubmed-meshheading:10506186-Chromosome Mapping, pubmed-meshheading:10506186-Cloning, Molecular, pubmed-meshheading:10506186-Cytoplasm, pubmed-meshheading:10506186-Cytoskeletal Proteins, pubmed-meshheading:10506186-Fluorescent Antibody Technique, pubmed-meshheading:10506186-Gene Expression Regulation, Developmental, pubmed-meshheading:10506186-In Situ Hybridization, Fluorescence, pubmed-meshheading:10506186-Mice, pubmed-meshheading:10506186-Molecular Sequence Data, pubmed-meshheading:10506186-Muscle, Skeletal, pubmed-meshheading:10506186-Muscle Proteins, pubmed-meshheading:10506186-Myocardium, pubmed-meshheading:10506186-RNA, Messenger, pubmed-meshheading:10506186-Rats, pubmed-meshheading:10506186-Recombinant Fusion Proteins, pubmed-meshheading:10506186-Regeneration, pubmed-meshheading:10506186-Sequence Homology, Amino Acid, pubmed-meshheading:10506186-X Chromosome, pubmed-meshheading:10506186-src Homology Domains
pubmed:year
1999
pubmed:articleTitle
Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain.
pubmed:affiliation
Department of Genetics, University of Torino, Torino 10126, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't