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(Received for publication, January 24, 1997)
From the Department of Cell Biology, University of Alabama at
Birmingham, Birmingham, Alabama 35294
During cell-matrix adhesion, both tyrosine and
serine/threonine kinases are activated. Integrin ligation correlates
with tyrosine phosphorylation, whereas the later stages of spreading
and focal adhesion and stress fiber formation in primary fibroblasts
requires interactions of cell surface proteoglycan with heparin-binding moieties. This correlates with protein kinase C (PKC) activation, and
PKC
can become localized to focal adhesions in normal, but not
transformed, cells. PKC activation has been thought to be downstream of
initial receptor-ligand interactions. We now show, however, that
syndecan-4 transmembrane heparan sulfate proteoglycan and PKC
co-immunoprecipitate and co-patch in vivo. The core protein of syndecan-4 can directly bind the catalytic domain of PKC and potentiate its activation by phospholipid mediators. It can also directly activate PKC in the absence of other mediators. This activity resides in the sequence LGKKPIYKK in the center of the short
cytoplasmic domain, and other syndecans lack this sequence and PKC
regulatory properties. Syndecan-4 is a focal adhesion component, and
this interaction may both localize PKC and amplify its activity at
sites of forming adhesions. This represents the first report of direct
transmembrane signaling through cell surface proteoglycans.
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