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J. Biol. Chem., Vol. 278, Issue 17, 15040-15048, April 25, 2003
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From the The protein-tyrosine kinase Pyk2/CAK
Interaction of the Tyrosine Kinase Pyk2 with the
N-Methyl-D-aspartate Receptor Complex via the
Src Homology 3 Domains of PSD-95 and SAP102*
§,§,§
Department of Pharmacology, University of
Wisconsin, Madison, Wisconsin 53706-1532, the § Department
of Pharmacology, University of Iowa, Iowa City, Iowa 52242-1109, and
the ¶ Department of Cell and Developmental Biology and
the Neuroscience Center, University of North Carolina,
Chapel Hill, North Carolina 27599
/CADTK is
a key activator of Src in many cells. At hippocampal synapses,
induction of long term potentiation requires the Pyk2/Src signaling
pathway, which up-regulates the activity of
N-methyl-D-aspartate-type glutamate receptors.
Because localization of protein kinases close to their substrates is
crucial for effective phosphorylation, we investigated how Pyk2 might
be recruited to the N-methyl-D-aspartate
receptor complex. This interaction is mediated by PSD-95 and its
homolog SAP102. Both proteins colocalize with Pyk2 at postsynaptic
dendritic spines in the cerebral cortex. The proline-rich regions in
the C-terminal half of Pyk2 bind to the SH3 domain of PSD-95 and
SAP102. The SH3 and guanylate kinase homology (GK) domain of PSD-95 and SAP102 interact intramolecularly, but the physiological significance of
this interaction has been unclear. We show that Pyk2 effectively binds
to the Src homology 3 (SH3) domain of SAP102 only when the GK domain is
removed from the SH3 domain. Characterization of PSD-95 and SAP102 as
adaptor proteins for Pyk2 fills a critical gap in the understanding of
the spatial organization of the Pyk2-Src signaling pathway at the
postsynaptic site and reveals a physiological function of the
intramolecular SH3-GK domain interaction in SAP102.
*
This work was supported by National Institutes of Health
Research Grants NS35563 (to J. W. H.), AG17502 (to J. W. H.), and NS39444 (to R. J. 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 correspondence should be addressed: Dept. of
Pharmacology, University of Iowa, 51 Newton Rd., Iowa City, IA
52242-1109. Tel.: 319-384-4732; Fax: 319-335-8930; E-mail:
johannes-hell@uiowa.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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