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Biochem Biophys Res Commun. 2002 Dec 6;299(3):510-5.

Phosphorylation of Bruton's tyrosine kinase by c-Abl.

Author information

1
Clinical Research Center, Karolinska Institutet, Huddinge University Hospital, Huddinge, Sweden. Magnus.Backesjo@crc.ki.se

Erratum in

  • Biochem Biophys Res Commun. 2003 Jan 31;301(1):259.

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.

PMID:
12445832
[Indexed for MEDLINE]

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