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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2003-6-9
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pubmed:abstractText |
Mammalian Enabled (Mena) is a mammalian homologue of Drosophila Enabled (Ena), which genetically interacts with Drosophila Abl tyrosine kinase. The signaling pathway involving c-Abl and Mena (Ena) is not fully understood. To find molecules that participate in the c-Abl/Mena pathway, we searched for Mena-binding proteins using a yeast two-hybrid system. We identified Abl interactor 1 (Abi-1), which is known to interact with c-Abl, as a binding protein for Mena. Binding analysis revealed that the Ena/Vasp homology 1 domain of Mena and the polyproline structure of Abi-1 are necessary for the interaction. The interaction between Mena and Abi-1 was also observed in a mammalian expression system. Importantly, Abi-1 dramatically promoted c-Abl-mediated tyrosine phosphorylation of Mena but not other substrates such as c-Cbl. Mutational analysis demonstrated that the phosphorylation site of Mena is Tyr-296. Our results suggest that Abi-1 regulates c-Abl-mediated phosphorylation of Mena by interacting with both proteins.
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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/ABI1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Abi1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ENA/VASP proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enah protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-abl,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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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 |
13
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21685-92
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12672821-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12672821-Alternative Splicing,
pubmed-meshheading:12672821-Amino Acid Sequence,
pubmed-meshheading:12672821-Animals,
pubmed-meshheading:12672821-Binding Sites,
pubmed-meshheading:12672821-Carrier Proteins,
pubmed-meshheading:12672821-Cell Line,
pubmed-meshheading:12672821-Cytoskeletal Proteins,
pubmed-meshheading:12672821-DNA, Complementary,
pubmed-meshheading:12672821-DNA Mutational Analysis,
pubmed-meshheading:12672821-DNA-Binding Proteins,
pubmed-meshheading:12672821-Gene Library,
pubmed-meshheading:12672821-Glutathione Transferase,
pubmed-meshheading:12672821-Homeodomain Proteins,
pubmed-meshheading:12672821-Humans,
pubmed-meshheading:12672821-Mice,
pubmed-meshheading:12672821-Microscopy, Fluorescence,
pubmed-meshheading:12672821-Molecular Sequence Data,
pubmed-meshheading:12672821-Phosphorylation,
pubmed-meshheading:12672821-Protein Binding,
pubmed-meshheading:12672821-Protein Structure, Tertiary,
pubmed-meshheading:12672821-Proto-Oncogene Proteins c-abl,
pubmed-meshheading:12672821-Rats,
pubmed-meshheading:12672821-Recombinant Fusion Proteins,
pubmed-meshheading:12672821-Sequence Homology, Amino Acid,
pubmed-meshheading:12672821-Signal Transduction,
pubmed-meshheading:12672821-Two-Hybrid System Techniques,
pubmed-meshheading:12672821-Tyrosine
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pubmed:year |
2003
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pubmed:articleTitle |
Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase.
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pubmed:affiliation |
School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan. tani@ls.toyaku.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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