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(Received for publication, March 18, 1996, and in revised form, April 23, 1996)
From the Departments of Biochemistry and Expression of the human immunodeficiency virus (HIV)
Nef protein has been linked to both decreased cell surface expression
of CD4 and an impairment of signal transduction. The recently reported
association of Nef with an unidentified serine kinase provides a clue
as to how Nef might exert its effects. Considering the key role of
protein kinase C (PKC) in T cell activation, we investigated the
possibility that Nef interacts with PKC. Our results, using two
approaches for detecting interactions between Nef and PKC isozymes in
Jurkat cells, show that Nef interacts preferentially with
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16753-16757
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
and
Molecular
Pharmacology, Beckman Center and Stanford University School of
Medicine, Stanford, California 94305
PKC. The
interaction of Nef and PKC is independent of calcium,
enhanced by phospholipid activators of PKC and not affected by a
PKC pseudosubstrate peptide. Phorbol 12-myristate 13-acetate and
phytohemagglutinin stimulation of Jurkat cells expressing Nef fails to
produce the usual translocation of PKC from the cytosol to the
particulate fraction; translocation of 
PKC and 
PKC was
unaffected. Indeed, there appears to be a net loss of PKC in
Nef-expressing cells following stimulation. The loss of PKC, which
may be a result of inhibition of its binding to RACKs due to Nef
binding, could contribute to the various impairments of T cell function
associated with HIV infection and Nef expression.
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