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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2002-2-20
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pubmed:abstractText |
The targeting of mRNA and local protein synthesis is important for the generation and maintenance of cell polarity. As part of the translational machinery as well as an actin/microtubule-binding protein, elongation factor 1alpha (EF1alpha) is a candidate linker between the protein translation apparatus and the cytoskeleton. We demonstrate in this work that EF1alpha colocalizes with beta-actin mRNA and F-actin in protrusions of chicken embryo fibroblasts and binds directly to F-actin and beta-actin mRNA simultaneously in vitro in actin cosedimentation and enzyme-linked immunosorbent assays. To investigate the role of EF1alpha in mRNA targeting, we mapped the two actin-binding sites on EF1alpha at high resolution and defined one site at the N-terminal 49 residues of domain I and the other at the C-terminal 54 residues of domain III. In vitro actin-binding assays and localization in vivo of recombinant full-length EF1alpha and its various truncates demonstrated that the C terminus of domain III was the dominant actin-binding site both in vitro and in vivo. We propose that the EF1alpha-F-actin complex is the scaffold that is important for beta-actin mRNA anchoring. Disruption of this complex would lead to delocalization of the mRNA. This hypothesis was tested by using two dominant negative polypeptides: the actin-binding domain III of EF1alpha and the EF1alpha-binding site of yeast Bni1p, a protein that inhibits EF1alpha binding to F-actin and also is required for yeast mRNA localization. We demonstrate that either domain III of EF1alpha or the EF1alpha-binding site of Bni1p inhibits EF1alpha binding to beta-actin mRNA in vitro and causes delocalization of beta-actin mRNA in chicken embryo fibroblasts. Taken together, these results implicate EF1alpha in the anchoring of beta-actin mRNA to the protrusion in crawling cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-10209102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-10504297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-11416185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-11470405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1296758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1360014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-15157465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1637873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1666339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1852137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1891715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-1993736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-2071586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-3698103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-4040521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-6260369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7197276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7286081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7593319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7610475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7750521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7821209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7914201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-7929587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8063858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8063859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8366129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-837445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8408195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8521618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8625407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8743583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8913639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8922379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8937988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-8947553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9082982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9087442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9184220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9214622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9219698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9405304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9412505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9415374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9553081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11854414-9591785
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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 |
Feb
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
579-92
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11854414-Actins,
pubmed-meshheading:11854414-Animals,
pubmed-meshheading:11854414-Binding Sites,
pubmed-meshheading:11854414-Cells, Cultured,
pubmed-meshheading:11854414-Cytoskeleton,
pubmed-meshheading:11854414-Peptide Elongation Factor 1,
pubmed-meshheading:11854414-Protein Binding,
pubmed-meshheading:11854414-Protein Structure, Tertiary,
pubmed-meshheading:11854414-RNA, Messenger,
pubmed-meshheading:11854414-Rats
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pubmed:year |
2002
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pubmed:articleTitle |
Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions.
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pubmed:affiliation |
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, New York, New York 10461, USA. liug@mail.amc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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