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J Biol Chem, Vol. 273, Issue 40, 25548-25551, October 2, 1998
From the Angiogenesis Research Center, Cardiovascular Division,
Department of Medicine, Beth Israel Deaconess Medical Center, Harvard
Medical School, Boston, Massachusetts 02215
Syndecans are transmembrane proteoglycans capable
of carrying both heparan and chondroitin sulfate chains. The
cytoplasmic tail of syndecan-4 was recently reported to undergo
in vivo phosphorylation on Ser183 in the
membrane-proximal part of the tail (Horowitz, A., and Simons, M. (1998)
J. Biol. Chem. 273, 10914-10918). However, the functional consequences of this event remain unknown. The cytoplasmic tail of syndecan-4 is known to undergo multimerization and to activate
protein kinase C
(PKC), with both events depending on the
presence of the commonly occurring phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2). In the present investigation we
found that phosphorylation of Ser183 produced a 10-fold
reduction in the ability of syndecan-4 to activate PKC, without
affecting its ability to bind the PKC. Because Ser183 is
adjacent to positively charged lysine groups that resemble PIP2-binding regions in several other proteins,
phosphorylation of this serine may affect the binding affinity of the
syndecan-4 cytoplasmic tail to PIP2. We found that the
Ser183-phosphorylated cytoplasmic tail of syndecan-4 has
indeed a significantly lower affinity to PIP2 compared with
the nonphosphorylated tail. Furthermore, Ser183
phosphorylation abolished PIP2-dependent
oligomerization of syndecan-4 cytoplasmic tails. We conclude that
Ser183 phosphorylation regulates
syndecan-4-dependent activation of PKC by reducing the
affinity to PIP2 and inhibiting the oligomerization of
syndecan-4 cytoplasmic tails. These results further support the role of
syndecan-4 in signal transduction in endothelial cells.
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