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J Biol Chem, Vol. 274, Issue 38, 27039-27046, September 17, 1999
IIPKC
§,§
**, and§
From the § Ernest Gallo Research Center, the Departments
of Protein kinase C (PKC) isozymes move upon
activation from one intracellular site to another. PKC-binding
proteins, such as receptors for activated C kinase (RACKs), play an
important role in regulating the localization and diverse functions of
PKC isozymes. RACK1, the receptor for activated Neurology, Cellular and Molecular
Pharmacology, and ** Pediatrics, and the
Neuroscience Graduate Program and Center
for Neurobiology of Addiction, University of California, San
Francisco, California 94110-3518
IIPKC, determines
the localization and functional activity of IIPKC. However, the
mechanism by which RACK1 localizes activated IIPKC is not known.
Here, we provide evidence that the intracellular localization of RACK1
changes in response to PKC activation. In Chinese hamster ovary cells transfected with the dopamine D2L receptor and in NG108-15 cells, PKC
activation by either phorbol ester or a dopamine D2 receptor agonist
caused the movement of RACK1. Moreover, PKC activation resulted in the
in situ association and movement of RACK1 and IIPKC to
the same intracellular sites. Time course studies indicate that PKC
activation induces the association of the two proteins prior to their
co-movement. We further show that association of RACK1 and IIPKC is
required for the movement of both proteins. Our results suggest that
RACK1 is a PKC shuttling protein that moves IIPKC from one
intracellular site to another.
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