|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1998-5-14
|
|
pubmed:abstractText |
The myofibrils of cross-striated muscle fibers contain in their M bands cytoskeletal proteins whose main function seems to be the stabilization of the three-dimensional arrangement of thick filaments. We identified two immunoglobin domains (Mp2-Mp3) of M-protein as a site binding to the central region of light meromyosin. This binding is regulated in vitro by phosphorylation of a single serine residue (Ser76) in the immediately adjacent amino-terminal domain Mp1. M-protein phosphorylation by cAMP-dependent kinase A inhibits binding to myosin LMM. Transient transfection studies of cultured cells revealed that the myosin-binding site seems involved in the targeting of M-protein to its location in the myofibril. Using the same method, a second myofibril-binding site was uncovered in domains Mp9-Mp13. These results support the view that specific phosphorylation events could be also important for the control of sarcomeric M band formation and remodeling.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1384035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1396662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1400348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1696729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1704877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-194899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1956315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-1956339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2065865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2453516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2474551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2478565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2722778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-2999980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-3305014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-3305119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-3888375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-3905857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-4044641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-4093497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-4209974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-6189843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-6204858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-6350609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-6537951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-6731838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-708756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-731697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-7505783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-7588733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-8308058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-8404852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-8631348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-8741211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-8830773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9529381-9029142
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1059-1524
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
9
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
829-40
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9529381-Amino Acid Sequence,
pubmed-meshheading:9529381-Animals,
pubmed-meshheading:9529381-Binding Sites,
pubmed-meshheading:9529381-Cattle,
pubmed-meshheading:9529381-Cells, Cultured,
pubmed-meshheading:9529381-Cricetinae,
pubmed-meshheading:9529381-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:9529381-Mice,
pubmed-meshheading:9529381-Molecular Sequence Data,
pubmed-meshheading:9529381-Muscle Proteins,
pubmed-meshheading:9529381-Myeloma Proteins,
pubmed-meshheading:9529381-Myofibrils,
pubmed-meshheading:9529381-Myosins,
pubmed-meshheading:9529381-Phosphorylation,
pubmed-meshheading:9529381-Recombinant Proteins,
pubmed-meshheading:9529381-Sarcomeres,
pubmed-meshheading:9529381-Transfection
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band.
|
|
pubmed:affiliation |
Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, D-37077 Göttingen, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
