Source:http://linkedlifedata.com/resource/pubmed/id/17194709
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2007-3-12
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pubmed:databankReference | |
pubmed:abstractText |
In addition to regulating cell motility, contractility, and cytokinesis, the actin cytoskeleton plays a critical role in the regulation of transcription and gene expression. We have previously identified a novel muscle-specific actin-binding protein, STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. To further dissect the STARS/SRF pathway, we performed a yeast two-hybrid screen of a skeletal muscle cDNA library using STARS as bait, and we identified two novel members of the ABLIM protein family, ABLIM-2 and -3, as STARS-interacting proteins. ABLIM-1, which is expressed in retina, brain, and muscle tissue, has been postulated to function as a tumor suppressor. ABLIM-2 and -3 display distinct tissue-specific expression patterns with the highest expression levels in muscle and neuronal tissue. Moreover, these novel ABLIM proteins strongly bind F-actin, are localized to actin stress fibers, and synergistically enhance STARS-dependent activation of SRF. Conversely, knockdown of endogenous ABLIM expression utilizing small interfering RNA significantly blunted SRF-dependent transcription in C2C12 skeletal muscle cells. These findings suggest that the members of the novel ABLIM protein family may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BarrientosTomasaT,
pubmed-author:Bassel-DubyRhondaR,
pubmed-author:BezprozvannayaSvetlanaS,
pubmed-author:FrankDerkD,
pubmed-author:FreyNorbertN,
pubmed-author:KatusHugo AHA,
pubmed-author:KuwaharaKoichiroK,
pubmed-author:OlsonEric NEN,
pubmed-author:PipesG C TegGC,
pubmed-author:RichardsonJames AJA
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8393-403
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17194709-Actins,
pubmed-meshheading:17194709-Amino Acid Sequence,
pubmed-meshheading:17194709-Animals,
pubmed-meshheading:17194709-COS Cells,
pubmed-meshheading:17194709-Cercopithecus aethiops,
pubmed-meshheading:17194709-Humans,
pubmed-meshheading:17194709-LIM Domain Proteins,
pubmed-meshheading:17194709-Mice,
pubmed-meshheading:17194709-Microfilament Proteins,
pubmed-meshheading:17194709-Molecular Sequence Data,
pubmed-meshheading:17194709-Muscle, Skeletal,
pubmed-meshheading:17194709-Protein Binding,
pubmed-meshheading:17194709-Retina,
pubmed-meshheading:17194709-Sequence Homology, Amino Acid,
pubmed-meshheading:17194709-Signal Transduction,
pubmed-meshheading:17194709-Two-Hybrid System Techniques
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pubmed:year |
2007
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pubmed:articleTitle |
Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin.
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pubmed:affiliation |
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, 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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