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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 |
2000-1-11
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pubmed:abstractText |
Drebrin is an actin-binding protein which is expressed at highly levels in neurons. When introduced into fibroblasts, it has been known to bind to F-actin and to cause remodeling of F-actin. Here, we performed a domain analysis of the actin-binding and actin-remodeling activities of drebrin. Various fragments of drebrin cDNA were fused with green fluorescent protein cDNA and introduced into Chinese hamster ovary cells. Association of the fusion protein with F-actin and remodeling of the F-actin were examined. We found that the central 85-amino-acid sequence (residues 233-317) was sufficient for the binding to and remodeling of F-actin. The binding activity of this fragment was relatively low compared with that of full-length drebrin, but all the types of abnormalities of F-actin that are observed with full-length drebrin were also observed with this fragment. When this sequence was further fragmented, the actin-binding activity was greatly reduced and the actin-remodeling activity disappeared. The actin-binding activity of the central region of drebrin was confirmed by a cosedimentation assay of chymotryptic fragments of drebrin with purified actin. These data indicate that the actin-binding domain and actin-remodeling domain are identical and that this domain is located at the central region of drebrin.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/drebrins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
673-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10585290-Actins,
pubmed-meshheading:10585290-Animals,
pubmed-meshheading:10585290-Blotting, Western,
pubmed-meshheading:10585290-CHO Cells,
pubmed-meshheading:10585290-Chymotrypsin,
pubmed-meshheading:10585290-Cricetinae,
pubmed-meshheading:10585290-DNA, Complementary,
pubmed-meshheading:10585290-Genes, Reporter,
pubmed-meshheading:10585290-Green Fluorescent Proteins,
pubmed-meshheading:10585290-Indicators and Reagents,
pubmed-meshheading:10585290-Luminescent Proteins,
pubmed-meshheading:10585290-Microfilament Proteins,
pubmed-meshheading:10585290-Mutagenesis, Insertional,
pubmed-meshheading:10585290-Neuropeptides,
pubmed-meshheading:10585290-Peptide Fragments,
pubmed-meshheading:10585290-Phosphorylation,
pubmed-meshheading:10585290-Protein Binding,
pubmed-meshheading:10585290-Recombinant Fusion Proteins,
pubmed-meshheading:10585290-Stress, Mechanical
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pubmed:year |
1999
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pubmed:articleTitle |
Domain analysis of the actin-binding and actin-remodeling activities of drebrin.
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pubmed:affiliation |
Department of Neurobiology and Behavior, Department of Pharmacology, Gunma University School of Medicine, 3-39-22 Showamachi, Maebashi, 371, Japan. hayashi@sb.gunma-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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