Phosphorylation of Bruton's tyrosine kinase by c-Abl

Biochem Biophys Res Commun. 2002 Dec 6;299(3):510-5. doi: 10.1016/s0006-291x(02)02643-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agammaglobulinaemia Tyrosine Kinase
  • Amino Acid Motifs
  • Animals
  • Cell Line
  • Humans
  • Immunohistochemistry
  • Phosphorylation
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins c-abl / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • Tyrosine / metabolism
  • src Homology Domains


  • Recombinant Fusion Proteins
  • Tyrosine
  • Protein-Tyrosine Kinases
  • Agammaglobulinaemia Tyrosine Kinase
  • BTK protein, human
  • Proto-Oncogene Proteins c-abl