Source:http://linkedlifedata.com/resource/pubmed/id/12445832
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-11-26
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pubmed:abstractText |
Bruton's tyrosine kinase (Btk) is necessary for B-lymphocyte development. Mutation in the gene coding for Btk causes X-linked agammaglobulinemia (XLA) in humans. Similar to Btk, c-Abl is a tyrosine kinase shuttling between the cytoplasm and the nucleus where it is involved in different functions depending on the localization. In this report we describe for the first time that c-Abl and Btk physically interact and that c-Abl can phosphorylate tyrosine 223 in the SH3 domain of Btk. Interestingly, the Btk sequence matched a v-Abl substrate [correction] identified from a randomized peptide library and was also highly related to a number of previously found c-Abl substrates.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Agammaglobulinaemia tyrosine kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
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:author | |
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
510-5
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pubmed:dateRevised |
2011-11-2
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pubmed:articleTitle |
Phosphorylation of Bruton's tyrosine kinase by c-Abl.
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pubmed:affiliation |
Clinical Research Center, Karolinska Institutet, Huddinge University Hospital, Huddinge, Sweden. Magnus.Backesjo@crc.ki.se
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