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(Received for publication, May 30,
1995; and in revised form, August 3, 1995) The 14.3.3
Volume 270,
Number 40,
Issue of October 06, pp. 23681-23687, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Domains Important for Self-association and Raf Binding
protein is a ubiquitous and abundant
arachidonate-selective acyltransferase and putative phospholipase
A
, which self-assembles into dimers and binds to c-Raf-1
and other polypeptides in vitro and in intact cells. The
14.3.3 polypeptides endogenous to Sf9 cells associate in situ with both active and inactive recombinant Raf and copurify at a
fairly reproducible molar ratio that is probably 
1. Purified
baculoviral recombinant Raf, despite its preassociated 14.3.3
polypeptide, binds additional recombinant 14.3.3 polypeptide in vitro, in a saturable and specific reaction, forming a
complex that is resistant to 1 M LiCl. A two-hybrid analysis
indicates that 14.3.3
binds primarily to Raf noncatalytic
sequences distinct from those that bind Ras-GTP, and in vitro 14.3.3
binds to Raf without inhibiting the Ras-Raf
association or Raf-catalyzed MEK phosphorylation. Deletion analysis of
14.3.3
(1-245) indicates that the 14.3.3 domain responsible
for binding to Raf extends over the carboxyl-terminal 100 amino acids,
whereas 14.3.3 dimerization is mediated by amino-terminal sequences. As
with Ras, the 14.3.3
polypeptide does not activate purified Raf
directly in vitro. Moreover, expression of recombinant 14.3.3
in COS cells beyond the substantial level of endogenous 14.3.3
protein does not alter endogenous Raf kinase, as judged by the activity
of a cotransfected Erk-1 reporter. Coexpression of recombinant 14.3.3
with recombinant Myc-tagged Raf in COS cells does increase
substantially the Myc-Raf kinase activity achieved during transient
expression, which is attributable primarily to an increased level of
Myc-Raf polypeptide, without alteration of Myc-Raf specific activity or
the activation that occurs in response to epidermal growth factor or
12-O-tetradecanoylphorbol-13-acetate. Nevertheless, evidence
that 14.3.3 actively participates in Raf activation in situ is
provided by the finding that although full-length 14.3.3
binds
active Raf in situ, truncated versions of 14.3.3, some of
which bind Raf polypeptide in situ nearly as well as
full-length 14.3.3
, are recovered in association only with
inactive Raf polypeptides. Thus, 14.3.3 polypeptides bind tightly to
one or more sites on c-Raf. Overexpression of 14.3.3
enhances the
expression of recombinant Raf, perhaps by stabilizing the Raf
polypeptide. In addition, Raf polypeptides bound to truncated 14.3.3
polypeptides are unable to undergo activation in situ,
indicating that 14.3.3 participates in the process of Raf activation by
mechanisms that remain to be elucidated.
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