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rdf:type |
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lifeskim:mentions |
umls-concept:C0056248,
umls-concept:C0205099,
umls-concept:C0206427,
umls-concept:C0917705,
umls-concept:C1267092,
umls-concept:C1514562,
umls-concept:C1552915,
umls-concept:C1704675,
umls-concept:C1705186,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1947942,
umls-concept:C2347970,
umls-concept:C2347971
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pubmed:issue |
30
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pubmed:dateCreated |
2008-7-21
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pubmed:abstractText |
Actin-myosin II filament-based contractile structures in striated muscle, smooth muscle, and nonmuscle cells contain the actin filament-cross-linking protein alpha-actinin. In striated muscle Z-disks, alpha-actinin interacts with N-terminal domains of titin to provide a structural linkage crucial for the integrity of the sarcomere. We previously discovered a long titin isoform, originally smitin, hereafter sm-titin, in smooth muscle and demonstrated that native sm-titin interacts with C-terminal EF hand region and central rod R2-R3 spectrin-like repeat region sites in alpha-actinin. Reverse transcription-PCR analysis of RNA from human adult smooth muscles and cultured rat smooth muscle cells and Western blot analysis with a domain-specific antibody presented here revealed that sm-titin contains the titin gene-encoded Zq domain that may bind to the alpha-actinin R2-R3 central rod domain as well as Z-repeat domains that bind to the EF hand region. We investigated whether the sm-titin Zq domain binds to alpha-actinin R2 and R3 spectrin repeat-like domain loops that lie in proximity with two-fold symmetry on the surface of the central rod. Mutations in alpha-actinin R2 and R3 domain loop residues decreased interaction with expressed sm-titin Zq domain in glutathione S-transferase pull-down and solid phase binding assays. Alanine mutation of a region of the Zq domain with high propensity for alpha-helix formation decreased apparent Zq domain dimer formation and decreased Zq interaction with the alpha-actinin R2-R3 region in surface plasmon resonance assays. We present a model in which two sm-titin Zq domains interact with each other and with the two R2-R3 sites in the alpha-actinin central rod.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10618168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10685064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10819994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10956328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10987068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-10987078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11053363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11101506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11133929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11305911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11457815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11573089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11699871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11717165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-11781337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-12142273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-12569417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-1400592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15050827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15638516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15802564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15833278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15875052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-15923651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-16230110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-16531234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-16949617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-1700896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-17366640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-7767873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-9245597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-9473406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-9501083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-9817758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18519573-9887957
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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 |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20959-67
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18519573-Actinin,
pubmed-meshheading:18519573-Amino Acid Sequence,
pubmed-meshheading:18519573-Animals,
pubmed-meshheading:18519573-Aorta,
pubmed-meshheading:18519573-Binding Sites,
pubmed-meshheading:18519573-Chickens,
pubmed-meshheading:18519573-Female,
pubmed-meshheading:18519573-Humans,
pubmed-meshheading:18519573-Molecular Sequence Data,
pubmed-meshheading:18519573-Muscle, Smooth,
pubmed-meshheading:18519573-Muscle Proteins,
pubmed-meshheading:18519573-Protein Binding,
pubmed-meshheading:18519573-Protein Kinases,
pubmed-meshheading:18519573-Rats,
pubmed-meshheading:18519573-Sequence Homology, Amino Acid,
pubmed-meshheading:18519573-Swine,
pubmed-meshheading:18519573-Uterus
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pubmed:year |
2008
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pubmed:articleTitle |
Smooth muscle titin Zq domain interaction with the smooth muscle alpha-actinin central rod.
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pubmed:affiliation |
Department of Biological Science, College of Medicine, Florida State University, Tallahassee, FL 32306, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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