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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2009-2-23
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pubmed:abstractText |
The Z-line in each striated muscle has a precisely defined width that corresponds to muscle fiber type, and it can enlarge several fold in nemaline myopathy. To explore the mechanism(s) underlying Z-line width and structure maintenance, a series of sarcomeric-alpha-actinin mutants tagged with myc-epitope was transfected into cultured chick myotubes. By double-staining transfected myotubes with myc and myofibrillar protein antibodies, we found that alpha-actinin mutants with deletion of the region from the beginning of the fourth spectrin repeat to the start of the EF-hands resulted in expansion of Z-line width, often displayed a doublet staining pattern, and resulted in formation of nemaline-like bodies in older myotubes under fluorescence microscope. Yeast-two hybridization analysis demonstrated that this region was involved in vinculin binding, and for vinculin to bind alpha-actinin, residues 1-116 and 258-323 were required. Hence, we have defined a critical region of s-alpha-actinin that affects the width and integrity of the Z-line. This region is at least involved in the interaction with vinculin.
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pubmed:commentsCorrections |
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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 |
Mar
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pubmed:issn |
1090-2422
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
315
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
748-59
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19166831-Actinin,
pubmed-meshheading:19166831-Animals,
pubmed-meshheading:19166831-Avian Proteins,
pubmed-meshheading:19166831-Binding Sites,
pubmed-meshheading:19166831-Cells, Cultured,
pubmed-meshheading:19166831-Chick Embryo,
pubmed-meshheading:19166831-Chickens,
pubmed-meshheading:19166831-Gene Deletion,
pubmed-meshheading:19166831-Models, Biological,
pubmed-meshheading:19166831-Muscle Fibers, Skeletal,
pubmed-meshheading:19166831-Muscle Proteins,
pubmed-meshheading:19166831-Mutagenesis, Site-Directed,
pubmed-meshheading:19166831-Myopathies, Nemaline,
pubmed-meshheading:19166831-Protein Binding,
pubmed-meshheading:19166831-Protein Interaction Domains and Motifs,
pubmed-meshheading:19166831-Protein Interaction Mapping,
pubmed-meshheading:19166831-Protein Kinases,
pubmed-meshheading:19166831-Sarcomeres,
pubmed-meshheading:19166831-Spectrin,
pubmed-meshheading:19166831-Vinculin
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pubmed:year |
2009
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pubmed:articleTitle |
Sarcomeric-alpha-actinin defective in vinculin-binding causes Z-line expansion and nemaline-like body formation in cultured chick myotubes.
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pubmed:affiliation |
Key laboratory of Carcinogenesis and Translational Research (Ministry of Education), Clinical Research Laboratory, Beijing Cancer Hospital and Institute, Peking University School of Oncology, Beijing 100142, PR China. zlzqzhang@bjmu.edu.cn
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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