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Vol. 60, Issue 1, 63-70, July 2001
-Arrestin I, and Endocytic
Processing
Department of Physiology and Pharmacology, Strathclyde Institute
for Biomedical Sciences, University of Strathclyde, Glasgow, Scotland,
United Kingdom
In this study, we have shown that nerve growth factor (NGF)-dependent
activation of the p42/p44 mitogen-activated protein kinase (p42/p44
MAPK) pathway in PC12 cells can be partially blocked by pertussis toxin
(which inactivates the G proteins Gi/o). This suggests that
the Trk A receptor may use a G protein-coupled receptor pathway to
signal to p42/p44 MAPK. This was supported by data showing that the
NGF-dependent activation of p42/p44 MAPK is potentiated in cells
transfected with G protein-coupled receptor kinase 2 (GRK2) or
-arrestin I. Moreover, GRK2 is constitutively bound with the Trk A
receptor, whereas NGF stimulates the pertussis toxin-sensitive binding
of -arrestin I to the TrkA receptor-GRK2 complex. Both GRK2 and
-arrestin I are involved in clathrin-mediated endocytic signaling to
p42/p44 MAPK. Indeed, inhibitors of clathrin-mediated endocytosis
(e.g., monodansylcadaverine, concanavalin A, and hyperosmolar sucrose)
reduced the NGF-dependent activation of p42/p44 MAPK. Finally, we have
found that the G protein-coupled receptor-dependent component
regulating p42/p44 MAPK is required for NGF-induced differentiation of
PC12 cells. Thus, NGF-dependent inhibition of DNA synthesis was
partially blocked by PD098059 (inhibitor of MAPK kinase-1 activation)
and pertussis toxin. Our findings are the first to show that the Trk A
receptor uses a classic G protein-coupled receptor-signaling
pathway to promote differentiation of PC12 cells.
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