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J Biol Chem, Vol. 274, Issue 28, 19752-19761, July 9, 1999
From the Division of Allergy, La Jolla Institute for Allergy and
Immunology, San Diego, California 92121, the § Division
of Experimental Medicine, Brigham and Women's Hospital,
Boston, Massachusetts 02115, the ¶ Department of Molecular and
Experimental Medicine, The Scripps Research Institute,
La Jolla, California 92037, and the A fraction of Bruton's tyrosine kinase (Btk)
co-localizes with actin fibers upon stimulation of mast cells via the
high affinity IgE receptor (Fc
Pleckstrin Homology Domains Interact with Filamentous Actin
, Department of Clinical
Molecular Biology, Faculty of Medicine, Kyoto University, Kawahara-cho
Shogoin, Sakyo-ku, Kyoto 606, Japan
RI). In this study, a molecular basis
of the Btk co-localization with actin fibers is presented. Btk and
other Tec family tyrosine kinases have a pleckstrin homology (PH)
domain at their N termini. The PH domain is a short peptide module
frequently found in signal-transducing proteins and cytoskeletal
proteins. Filamentous actin (F-actin) is shown to be a novel ligand for a subset of PH domains, including that of Btk. The actin-binding site
was mapped to a 10-residue region of the N-terminal region of Btk.
Basic residues in this short stretch are demonstrated to be involved in
actin binding. Isolated PH domains induced actin filament bundle
formation. Consistent with these observations, Btk binds F-actin
in vitro and in vivo. Wild-type Btk protein is
in part translocated to the cytoskeleton upon FcRI cross-linking, whereas Btk containing a mutated PH domain is not.
Phosphatidylinositol 3,4,5-trisphosphate-mediated membrane
translocation of Btk was enhanced in cytochalasin
D-pretreated, FcRI-stimulated mast cells. These data
indicate that PH domain-mediated F-actin binding plays a role in Btk
co-localization with actin filaments.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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