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Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 2003-2012
Involvement of Wiskott-Aldrich Syndrome Protein in B-Cell Cytoplasmic
Tyrosine Kinase Pathway
Yoshihiro Baba,
Shigeaki Nonoyama,
Masato Matsushita,
Tomoki Yamadori,
Shoji Hashimoto,
Kohsuke Imai,
Shigeyuki Arai,
Toshio Kunikata,
Masashi Kurimoto,
Tomohiro Kurosaki,
Hans D. Ochs,
Jun-ichi Yata,
Tadamitsu Kishimoto, and
Satoshi Tsukada
From the Department of Medicine III, Osaka University Medical School,
Osaka, Japan; the Department of Pediatrics, School of Medicine, Tokyo
Medical and Dental University, Tokyo, Japan; the Fujisaki Institute,
Hayashibara Biochemical Laboratories Inc, Okayama, Japan; the
Department of Molecular Genetics, Institute for Hepatic Research,
Kansai Medical University, Osaka, Japan; and the Department of
Pediatrics, School of Medicine, University of Washington, Seattle, WA.
Bruton's tyrosine kinase (Btk) has been shown to play a role in
normal B-lymphocyte development. Defective expression of Btk leads to
human and murine immunodeficiencies. However, the exact role of Btk in
the cytoplasmic signal transduction in B cells is still unclear. This
study represents a search for the substrate for Btk in vivo. We
identified one of the major phosphoproteins associated with Btk in the
preB cell line NALM6 as the Wiskott-Aldrich syndrome protein (WASP),
the gene product responsible for Wiskott-Aldrich syndrome, which is
another hereditary immunodeficiency with distinct abnormalities in
hematopoietic cells. We demonstrated that WASP was transiently
tyrosine-phosphorylated after B-cell antigen receptor cross-linking on
B cells, suggesting that WASP is located downstream of cytoplasmic
tyrosine kinases. An in vivo reconstitution system demonstrated that
WASP is physically associated with Btk and can serve as the substrate
for Btk. A protein binding assay suggested that the
tyrosine-phosphorylation of WASP alters the association between WASP
and a cellular protein. Furthermore, identification of the
phosphorylation site of WASP in reconstituted cells allowed us to
evaluate the catalytic specificity of Btk, the exact nature of which is
still unknown.
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