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Vol. 12, Issue 3, 615-627, March 2001
and
*Department of Cellular and Molecular Medicine, University of
California, San Diego, La Jolla, California 92093;
NGF initiates the majority of its neurotrophic effects by promoting
the activation of the tyrosine kinase receptor TrkA. Here we
describe a novel interaction between TrkA and GIPC, a PDZ domain protein. GIPC binds to the juxtamembrane region of TrkA through its PDZ
domain. The PDZ domain of GIPC also interacts with GAIP, an RGS
(regulators of G protein signaling) protein. GIPC and GAIP are
components of a G protein-coupled signaling complex thought to be
involved in vesicular trafficking. In transfected HEK 293T cells GIPC,
GAIP, and TrkA form a coprecipitable protein complex. Both TrkA and
GAIP bind to the PDZ domain of GIPC, but their binding sites within the
PDZ domain are different. The association of endogenous GIPC with the
TrkA receptor was confirmed by coimmunoprecipitation in PC12 (615)
cells stably expressing TrkA. By immunofluorescence GIPC colocalizes
with phosphorylated TrkA receptors in retrograde transport vesicles
located in the neurites and cell bodies of differentiated PC12 (615)
cells. These results suggest that GIPC, like other PDZ domain proteins,
serves to cluster transmembrane receptors with signaling molecules.
When GIPC is overexpressed in PC12 (615) cells, NGF-induced
phosphorylation of mitogen-activated protein (MAP) kinase
(Erk1/2) decreases; however, there is no effect on phosphorylation of
Akt, phospholipase C-Skirball Institute of Biomolecular Medicine, New York
University, New York, New York 10016; and §Department of
Psychiatry, Weill Medical College of Cornell University, New York, New
York 10021
1, or Shc. The association of TrkA receptors
with GIPC and GAIP plus the inhibition of MAP kinase by GIPC suggests
that GIPC may provide a link between TrkA and G protein signaling pathways.
X.L. and H.Y. contributed equally to this work.
Corresponding author. E-mail address:
mfarquhar{at}ucsd.edu.
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