Source:http://linkedlifedata.com/resource/pubmed/id/10320340
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
1999-6-7
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pubmed:abstractText |
N-RAP is a recently discovered muscle-specific protein that is concentrated at the myotendon junctions in skeletal muscle and at the intercalated disks in cardiac muscle. The C-terminal half of N-RAP contains a region with sequence homology to nebulin, while a LIM domain is found at its N-terminus. N-RAP is hypothesized to perform an anchoring function, linking the terminal actin filaments of myofibrils to protein complexes located beneath the sarcolemma. We used a solid-phase assay to screen myofibrillar and junctional proteins for binding to several recombinant fragments of N-RAP, including the nebulin-like super repeat region (N-RAP-SR), the N-terminal half including the LIM domain (N-RAP-NH), and the region of N-RAP between the super repeat region and the LIM domain (N-RAP-IB). Actin is the only myofibrillar protein tested that exhibits specific binding to N-RAP, with high-affinity binding to N-RAP super repeats, and 10-fold weaker binding to N-RAP-IB. In contrast, myosin, isolated myosin heads, tropomyosin, and troponin exhibited no specific interaction with N-RAP domains. A recombinant fragment corresponding to the C-terminal one-fourth of vinculin also binds specifically to N-RAP super repeats, while no specific N-RAP binding activity was observed for other regions of the vinculin molecule. Finally, talin binds with high affinity to the LIM domain of N-RAP. These results support our hypothesis that N-RAP is part of a complex of proteins that anchors the terminal actin filaments of the myofibril to the membrane, and functions in transmitting tension from the myofibrils to the extracellular matrix.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nrap protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Talin,
http://linkedlifedata.com/resource/pubmed/chemical/Vinculin,
http://linkedlifedata.com/resource/pubmed/chemical/nebulin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6135-43
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pubmed:dateRevised |
2004-11-18
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pubmed:meshHeading |
pubmed-meshheading:10320340-Actins,
pubmed-meshheading:10320340-Animals,
pubmed-meshheading:10320340-Antibodies,
pubmed-meshheading:10320340-Cell Membrane,
pubmed-meshheading:10320340-Mice,
pubmed-meshheading:10320340-Muscle Proteins,
pubmed-meshheading:10320340-Muscles,
pubmed-meshheading:10320340-Myofibrils,
pubmed-meshheading:10320340-Osmolar Concentration,
pubmed-meshheading:10320340-Sarcolemma,
pubmed-meshheading:10320340-Talin,
pubmed-meshheading:10320340-Vinculin
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pubmed:year |
1999
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pubmed:articleTitle |
Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks.
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pubmed:affiliation |
Laboratory of Physical Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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