The interplay between cyclin-B-Cdc2 kinase (MPF) and MAP kinase during maturation of oocytes

2001 ◽  
Vol 114 (2) ◽  
pp. 257-267 ◽  
Author(s):  
A. Abrieu ◽  
M. Doree ◽  
D. Fisher

Throughout oocyte maturation, and subsequently during the first mitotic cell cycle, the MAP kinase cascade and cyclin-B-Cdc2 kinase are associated with the control of cell cycle progression. Many roles have been directly or indirectly attributed to MAP kinase and its influence on cyclin-B-Cdc2 kinase in different model systems; yet a principle theme does not emerge from the published literature, some of which is apparently contradictory. Interplay between these two kinases affects the major events of meiotic maturation throughout the animal kingdom, including the suppression of DNA replication, the segregation of meiotic chromosomes, and the prevention of parthenogenetic activation. Central to many of these events appears to be the control by MAP kinase of cyclin translation and degradation.

Cell ◽  
1996 ◽  
Vol 87 (3) ◽  
pp. 519-529 ◽  
Author(s):  
Nathalie Lamarche ◽  
Nicolas Tapon ◽  
Lisa Stowers ◽  
Peter D Burbelo ◽  
Pontus Aspenström ◽  
...  

1999 ◽  
Vol 277 (4) ◽  
pp. C652-C664 ◽  
Author(s):  
Nathalie Rivard ◽  
Marie-Josée Boucher ◽  
Claude Asselin ◽  
Gilles L’Allemain

The present report delineates the critical pathway in the G1 phase involved in downregulation of p27Kip1, a cyclin-dependent kinase inhibitor, which plays a pivotal role in controlling entry into the S phase of the cell cycle. In resting CCL39 fibroblasts and IEC-6 intestinal epithelial cells, protein levels of p27Kip1 were elevated but dramatically decreased on serum stimulation, along with hyperphosphorylation of pRb and increased CDK2 activity. In both cell types, expression of ras resulted in an increase of basal and serum-stimulated E2F-dependent transcriptional activity and a reduction in p27Kip1 protein levels as well. The role of the mitogen-activated protein (MAP) kinase cascade in p27Kip1 reduction and S phase reentry was reinforced by the blockades of serum-induced E2F-dependent transcriptional activity and p27Kip1 downregulation with the MKK-1/2 inhibitor PD-98059. In both cell lines, downregulation of p27Kip1 was associated with a repression of its synthesis, an event mediated by the p42/p44 MAP kinase pathway. Using an antisense approach, we demonstrated that p27Kip1 may control cell cycle exit in both cell types. These data indicate that activation of the MAP kinase cascade is required for S phase entry and p27Kip1 downregulation in fibroblasts and epithelial cells.


1996 ◽  
Vol 21 (5) ◽  
pp. 437-444 ◽  
Author(s):  
Yasuyoshi Nishida ◽  
Yoshihiro H. Inoue ◽  
Leo Tsuda ◽  
Takashi Adachi-Yamada ◽  
Young-Mi Lim ◽  
...  

2001 ◽  
Vol 21 (11) ◽  
pp. 3671-3683 ◽  
Author(s):  
John M. Schmitt ◽  
Philip J. S. Stork

ABSTRACT In many normal and transformed cell types, the intracellular second messenger cyclic AMP (cAMP) blocks the effects of growth factors and serum on mitogenesis, proliferation, and cell cycle progression. cAMP exerts these growth-inhibitory effects via inhibition of the mitogen-activated protein (MAP) kinase cascade. Here, using Hek293 and NIH 3T3 cells, we show that cAMP's inhibition of the MAP kinase cascade is mediated by the small G protein Rap1. Activation of Rap1 by cAMP induces the association of Rap1 with Raf-1 and limits Ras-dependent activation of ERK. In NIH 3T3 cells, Rap1 is required not only for cAMP's inhibition of ERK activation but for inhibition of cell proliferation and mitogenesis as well.


Oncogene ◽  
1998 ◽  
Vol 16 (21) ◽  
pp. 2803-2813 ◽  
Author(s):  
Rodney J Fiddes ◽  
Peter W Janes ◽  
Susan P Sivertsen ◽  
Robert L Sutherland ◽  
Elizabeth A Musgrove ◽  
...  

Genetics ◽  
1997 ◽  
Vol 147 (1) ◽  
pp. 19-32 ◽  
Author(s):  
Kathrin Schrick ◽  
Barbara Garvik ◽  
Leland H Hartwell

Abstract The mating process in yeast has two distinct aspects. One is the induction and activation of proteins required for cell fusion in response to a pheromone signal; the other is chemotropism, i.e., detection of a pheromone gradient and construction of a fusion site available to the signaling cell. To determine whether components of the signal transduction pathway necessary for transcriptional activation also play a role in chemotropism, we examined strains with null mutations in components of the signal transduction pathway for diploid formation, prezygote formation and the chemotropic process of mating partner discrimination when transcription was induced downstream of the mutation. Cells mutant for components of the mitogen-activated protein (MAP) kinase cascade (ste5, ste20, ste11, ste7 or fus3 kss1) formed diploids at a frequency 1% that of the wild-type control, but formed prezygotes as efficiently as the wild-type control and showed good mating partner discrimination, suggesting that the MAP kinase cascade is not essential for chemotropism. In contrast, cells mutant for the receptor (ste2) or the β or γ subunit (ste4 and stel8) of the G protein were extremely defective in both diploid and prezygote formation and discriminated poorly between signaling and nonsignaling mating partners, implying that these components are important for chemotropism.


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