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Vol. 60, Issue 1, 92-103, July 2001
Laboratory of Molecular Neurobiology, Centre for Addiction and
Mental Health, Toronto, Ontario, Canada; and Departments of
Pharmacology, Psychiatry, and Institute of Medical Science, University
of Toronto
The ability of dopamine D4 and D2 receptors to
activate extracellular signal-regulated kinases (ERKs) 1 and 2 was
compared using Chinese hamster ovary (CHO-K1) cells transfected with
D4.2, D4.4, D4.7, and
D2L receptors. Dopamine stimulation of D4 or
D2L receptors produced a transient, dose-dependent increase
in ERK1/2 activity. Receptor-specific activation of the ERK
mitogen-activated protein kinase (MAPK) pathway was confirmed using the
D2-like receptor-selective agonist quinpirole, whereas the
specific antagonist haloperidol blocked activation. MAPK stimulation
was dependent on a pertussis-toxin-sensitive G protein
(Gi/o). trans-Activation of the
platelet-derived growth factor (PDGF) receptor was an essential step in
D4 and D2L receptor-induced MAPK activation.
PDGF receptor-selective tyrosine kinase inhibitors tyrphostin A9 and
AG1295 abolished or significantly inhibited ERK1/2 activation by
D4 and D2L receptors. Dopamine stimulation of
the D4 receptor also produced a rapid increase in tyrosine
phosphorylation of the PDGF receptor-
. The Src-family tyrosine
kinase inhibitor PP2 blocked MAPK activation by dopamine; however, this
drug was also found to inhibit PDGF-BB-stimulated ERK activity and
autophosphorylation of the PDGF receptor-. Downstream signaling
pathways support the involvement of a receptor tyrosine kinase. The
phosphoinositide 3-kinase inhibitors wortmannin and LY294002, protein
kinase C inhibitors GF109203X and Calphostin C, dominant-negative
RasN17, and the MEK inhibitor PD98059 significantly attenuated or
abolished activation of MAPK by dopamine D4 and D2L receptors. Our results indicate that D4 and
D2L receptors activate the ERK kinase cascade by first
mobilizing signaling by the PDGF receptor, followed by the subsequent
activation of ERK1/2 by pathways associated with this receptor tyrosine kinase.
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