Follicle-stimulating hormone activates extracellular signal-regulated kinase but not extracellular signal-regulated kinase kinase through a 100-kDa phosphotyrosine phosphatase

被引:111
作者
Cottom, J
Salvador, LM
Maizels, ET
Reierstad, S
Park, Y
Carr, DW
Davare, MA
Hell, JW
Palmer, SS
Dent, P
Kawakatsu, H
Ogata, M
Hunzicker-Dunn, M
机构
[1] Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA
[2] Vet Affairs Med Ctr, Dept Cell & Mol Biol, Portland, OR 97201 USA
[3] Oregon Hlth & Sci Univ, Dept Cell & Mol Biol, Portland, OR 97201 USA
[4] Univ Wisconsin, Dept Pharmacol, Madison, WI 53706 USA
[5] Serono Reprod Biol Inst, Rockland, MA 02370 USA
[6] Virginia Commonwealth Univ, Richmond, VA 23298 USA
[7] Univ Calif San Francisco, Lug Biol Ctr, San Francisco, CA 94110 USA
[8] Osaka Univ, Sch Med, Biomed Res Ctr, Osaka 565, Japan
关键词
D O I
10.1074/jbc.M203901200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this report we sought to elucidate the mechanism by which the follicle-stimulating hormone (FSH) receptor signals to promote activation of the p42/p44 extracellular signal-regulated protein kinases (ERKs) in granulosa cells. Results show that the ERK kinase MEK and upstream intermediates Raf-1, Ras, Src, and L-type Ca2+ channels are already partially activated in vehicle-treated cells and that FSH does not further activate them. This tonic stimulatory pathway appears to be restrained at the level of ERK by a 100-kDa phosphotyrosine phosphatase that associates with ERK in vehicle-treated cells and promotes dephosphorylation of its regulatory Tyr residue, resulting in ERK inactivation. FSH promotes the phosphorylation of this phosphotyrosine phosphatase and its dissociation from ERK, relieving ERK from inhibition and resulting in its activation by the tonic stimulatory pathway and consequent translocation to the nucleus. Consistent with this premise, FSH-stimulated ERK activation is inhibited by the cell-permeable protein kinase A-specific inhibitor peptide Myr-PKI as well as by inhibitors of MEK, Src, a Ca2+ channel blocker, and chelation of extracellular Ca2+. These results suggest that FSH stimulates ERK activity in immature granulosa cells by relieving an inhibition imposed by a 100-kDa phosphotyrosine phosphatase.
引用
收藏
页码:7167 / 7179
页数:13
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