Phosphorylation of Bruton's tyrosine kinase by c-Abl |
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Authors: | Bäckesjö Carl Magnus Vargas Leonardo Superti-Furga Giulio Smith C I |
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Institution: | Clinical Research Center, Karolinska Institutet, Huddinge University Hospital, Huddinge, Sweden. Magnus.Backesjo@crc.ki.se |
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Abstract: | 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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Keywords: | Bruton’s tyrosine kinase Btk c-Abl Tyrosine phosphorylation SH3 |
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