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(Received for publication, March 20, 1996, and in revised form, July 10, 1996)
From the Department of Microbiology, Mount Sinai School of
Medicine, New York, New York 10029
We previously identified a novel src-
and ras-suppressed gene, 322, encoding a
mitogenic regulatory function (Lin, X., Nelson, P. J., Frankfort, B.,
Tombler, E., Johnson, R., and Gelman, I. H. (1995) Mol. Cell.
Biol. 15, 2754-2762). Here, we characterize the 322
gene product as an in vivo and in vitro
substrate of protein kinase C (PKC). Hence, we named this product
SSeCKS (pronounced essex) for
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28430-28438
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
rc
uppr
ssed 
inase
ubstrate. Rabbit polyclonal sera raised against
glutathione S-transferase (GST)-SSeCKS recognized a
myristylated 280/290-kDa doublet in Rat-6 fibroblasts. SSeCKS levels in
src- and ras-transformed Rat-6 cells were 15-
and 8-fold less, respectively, than those in untransformed cells.
Short-term addition of phorbol ester resulted in a 5-fold increase in
SSeCKS phosphorylation which was inhibited by
bis-indolylmaleimide. In vitro phosphorylation
of GST-SSeCKS by purified rabbit brain PKC-
was enhanced by
phosphatidylserine and blocked by excess PKC pseudosubstrate inhibitor
peptide. GST-SSeCKS bound purified PKC- or PKC from Rat-6 lysates in
a phosphatidylserine-dependent manner. Four SSeCKS domains
containing Lys/Arg-rich motifs similar to the PKC phosphorylation site
in MARCKS were phosphorylated in vitro by PKC.
Immunofluorescence analysis showed SSeCKS present throughout the
cytoplasm with enrichment in podosomes and at the cell edge. Short-term
addition of phorbol esters caused the movement of SSeCKS from plasma
membrane sites to the perinucleus coincident with a loss of actin
stress fibers. These data suggest a role for SSeCKS in the control of
cellular cytoskeletal architecture.
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