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J. Biol. Chem., Vol. 276, Issue 48, 45207-45216, November 30, 2001
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From the § Department of Immunology and Rheumatology and
** Department of Molecular Systems, Merck Research
Laboratories, Rahway, New Jersey 07065, the B cell linker protein (BLNK) is a SLP-76-related
adaptor protein essential for signal transduction from the BCR. To
identify components of BLNK-associated signaling pathways, we performed a phosphorylation-dependent yeast two-hybrid analysis using
BLNK probes. Here we report that the serine/threonine kinase
hematopoietic progenitor kinase 1 (HPK1), which is activated upon
antigen-receptor stimulation and which has been implicated in the
regulation of MAP kinase pathways, interacts physically and
functionally with BLNK in B cells and with SLP-76 in T cells. This
interaction requires Tyr379 of HPK1 and the
Src homology 2 (SH2) domain of BLNK/SLP-76. Via homology
modeling, we defined a consensus binding site within ligands for SLP
family SH2 domains. We further demonstrate that the SH2 domain of
SLP-76 participates in the regulation of AP-1 and NFAT
activation in response to T cell receptor (TCR) stimulation and
that HPK1 inhibits AP-1 activation in a manner partially dependent on
its interaction with SLP-76. Our data are consistent with a model in
which full activation of HPK1 requires its own phosphorylation on
tyrosine and subsequent interaction with adaptors of the SLP family,
providing a mechanistic basis for the integration of this kinase into
antigen receptor signaling cascades.
Hematopoietic Progenitor Kinase 1 Associates
Physically and Functionally with the Adaptor Proteins B Cell Linker
Protein and SLP-76 in Lymphocytes*
§¶,
,,§§, and Department of
Medicine and Department of Microbiology and Immunology, Howard Hughes
Medical Institute, University of California, San Francisco, California
94143, and the Department of Pharmacology,
Rappaport Faculty of Medicine, Technion-Israel Institute of Technology,
POB 9649 Bat Galim, Haifa 31096, Israel
*
This work was supported in part by NCI, National Institutes
of Health, Grant RO1 CA72531 (to A. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom all correspondence should be addressed. Tel.:
732-594-4045; Fax: 732-594-5140; E-mail: Karsten_Sauer@Merck.com.
¶
These two authors contributed equally to this work.
§§
An investigator of the Howard Hughes Medical Institute.
¶¶
Present address: Amgen Inc., 1 Amgen Center Dr.,
Thousand Oaks, CA 91320.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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