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T3–1 Cell Line Is Mediated by Protein Kinase C, c-Src, and CDC42
Department of Biological Regulation (N.L.L., T.H., O.B., M.R.,
R.S.) The Weizmann Institute of Science Rehovot, 76100
Israel
Department of Biochemistry (M.R., D.H., N.R.,
Z.N.) George S. Wise Faculty of Life Sciences Tel Aviv
University Ramat Aviv 69978, Israel
The signaling of ligands operating via
heterotrimeric G proteins is mediated by a complex network that
involves sequential phosphorylation events. Signaling by the G
protein-coupled receptor GnRH was shown to include elevation of
Ca2+ and activation of phospholipases, protein
kinase C (PKC) and extracellular signal-regulated kinase (ERK). In this
study, GnRH was shown to activate Jun N-Terminal Kinase (JNK)/SAPK in
T3–1 cells in a PKC- and tyrosine kinase-dependent manner. GnRH as
well as tumor-promoting agent (TPA) also increased c-Src activity,
which peaked at 2 min after GnRH stimulation and was sensitive both to
PKC and to tyrosine kinase inhibitors. Coexpression of Csk, which
serves as a Src-dominant interfering kinase, and constitutively active
forms of Src, together with JNK, confirmed the involvement of c-Src
downstream of PKC in the GnRH-JNK pathway. Coexpression of dominant
negative and constitutively active forms of CDC42, Rac1, Ras, MEKK1,
and MEK1 with JNK indicated that JNK activation by GnRH and TPA is
mediated by CDC42 and MEKK1. Ras and MEK1, which are involved in a
related mitogen-activated protein kinase (MAPK) pathway, did not affect
JNK activation in T3–1 cells. Taken together, our results suggest
that GnRH stimulation of JNK activity is mediated by a unique pathway
that includes sequential activation of PKC, c-Src, CDC42, and probably
also MEKK1.
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