Source:http://linkedlifedata.com/resource/pubmed/id/11827972
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
2002-4-22
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pubmed:databankReference | |
pubmed:abstractText |
CasL/HEF1 belongs to the p130(Cas) family. It is tyrosine-phosphorylated following beta(1) integrin and/or T cell receptor stimulation and is thus considered to be important for immunological reactions. CasL has several structural motifs such as an SH3 domain and a substrate domain and interacts with many molecules through these motifs. To obtain more insights on the CasL-mediated signal transduction, we sought proteins that interact with the CasL SH3 domain by far Western screening, and we identified a novel human molecule, MICAL (a Molecule Interacting with CasL). MICAL is a protein of 118 kDa and is expressed in the thymus, lung, spleen, kidney, testis, and hematopoietic cells. MICAL has a calponin homology domain, a LIM domain, a putative leucine zipper motif, and a proline-rich PPKPP sequence. MICAL associates with CasL through this PPKPP sequence. MICAL is a cytoplasmic protein and colocalizes with CasL at the perinuclear area. Through the COOH-terminal region, MICAL also associates with vimentin that is a major component of intermediate filaments. Immunostaining revealed that MICAL localizes along with vimentin intermediate filaments. These results suggest that MICAL may be a cytoskeletal regulator that connects CasL to intermediate filaments.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/LIM Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Vimentin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14933-41
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11827972-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11827972-Amino Acid Sequence,
pubmed-meshheading:11827972-Base Sequence,
pubmed-meshheading:11827972-Cell Line,
pubmed-meshheading:11827972-Cytoskeletal Proteins,
pubmed-meshheading:11827972-DNA, Complementary,
pubmed-meshheading:11827972-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11827972-LIM Domain Proteins,
pubmed-meshheading:11827972-Microscopy, Fluorescence,
pubmed-meshheading:11827972-Molecular Sequence Data,
pubmed-meshheading:11827972-Plasmids,
pubmed-meshheading:11827972-Protein Binding,
pubmed-meshheading:11827972-RNA, Messenger,
pubmed-meshheading:11827972-Vimentin
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pubmed:year |
2002
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pubmed:articleTitle |
MICAL, a novel CasL interacting molecule, associates with vimentin.
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pubmed:affiliation |
Department of Hematology and Oncology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8655, Japan.
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pubmed:publicationType |
Journal Article
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