The activation of MAP kinase and p34cdc2/cyclin B during the meiotic maturation of Xenopus oocytes

2000 ◽  
pp. 131-143 ◽  
Author(s):  
Amparo Palmer ◽  
Angel R. Nebreda
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Cyclin B ◽  
Meiotic Maturation

scholarly journals Vg1RBP phosphorylation by Erk2 MAP kinase correlates with the cortical release of Vg1 mRNA during meiotic maturation of Xenopus oocytes

RNA ◽  
2009 ◽  
Vol 15 (6) ◽  
pp. 1121-1133 ◽  
Author(s):  
A. Git ◽  
R. Allison ◽  
E. Perdiguero ◽  
A. R. Nebreda ◽  
E. Houliston ◽  
...  
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Meiotic Maturation

Dissociation of MAP kinase activation and MPF activation in hormone-stimulated maturation of Xenopus oocytes

Development ◽  
1999 ◽  
Vol 126 (20) ◽  
pp. 4537-4546 ◽  
Author(s):  
D.L. Fisher ◽  
T. Brassac ◽  
S. Galas ◽  
M. Doree
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Kinase Activity ◽  
Early Response ◽  
Meiotic Maturation ◽  
Cdc2 Kinase ◽  
Kinase Activation ◽  
Cell Cycle Activation ◽  
Map Kinase Phosphatase ◽  
Universal Mechanism

MAP kinase activation occurs during meiotic maturation of oocytes from all animals, but the requirement for MAP kinase activation in reinitiation of meiosis appears to vary between different classes. In particular, it has become accepted that MAP kinase activation is necessary for progesterone-stimulated meiotic maturation of Xenopus oocytes, while this is clearly not the case in other systems. In this paper, we demonstrate that MAP kinase activation in Xenopus oocytes is an early response to progesterone and can be temporally dissociated from MPF activation. We show that MAP kinase activation can be suppressed by treatment with geldanamycin or by overexpression of the MAP kinase phosphatase Pyst1. A transient and low-level early activation of MAP kinase increases the efficiency of cell cycle activation later on, when MAP kinase activity is no longer essential. Many oocytes can still undergo reinitiation of meiosis in the absence of active MAP kinase. Suppression of MAP kinase activation does not affect the formation or activation of Cdc2-cyclin B complexes, but reduces the level of active Cdc2 kinase. We discuss these findings in the context of a universal mechanism for meiotic maturation in oocytes throughout the animal kingdom.

scholarly journals A p90rsk Mutant Constitutively Interacting with MAP Kinase Uncouples MAP Kinase from p34cdc2/Cyclin B Activation in Xenopus Oocytes

1999 ◽  
Vol 10 (9) ◽  
pp. 2971-2986 ◽  
Author(s):  
Anne-Claude Gavin ◽  
Aine Ni Ainle ◽  
Emanuele Chierici ◽  
Margaret Jones ◽  
Angel R. Nebreda
Keyword(s):  
Signal Transduction ◽  
Map Kinase ◽  
Oocyte Maturation ◽  
Xenopus Oocytes ◽  
Map Kinases ◽  
Cyclin B ◽  
Docking Site ◽  
Cdc25 Phosphatase ◽  
Cellular Processes ◽  
Sustained Activation

The efficient activation of p90rsk by MAP kinase requires their interaction through a docking site located at the C-terminal end of p90rsk. The MAP kinase p42mpk1 can associate with p90rsk in G2-arrested but not in mature Xenopusoocytes. In contrast, an N-terminally truncated p90rskmutant named D2 constitutively interacts with p42mpk1. In this report we show that expression of D2 inhibitsXenopus oocyte maturation. The inhibition requires the p42mpk1 docking site. D2 expression uncouples the activation of p42mpk1 and p34cdc2/cyclin B in response to progesterone but does not prevent signaling through p90rsk. Instead, D2 interferes with a p42mpk1-triggered pathway, which regulates the phosphorylation and activation of Plx1, a potential activator of the Cdc25 phosphatase. This new pathway that links the activation of p42mpk1 and Plx1 during oocyte maturation is independent of p34cdc2/cyclin B activity but requires protein synthesis. Using D2, we also provide evidence that the sustained activation of p42mpk1 can trigger nuclear migration in oocytes. Our results indicate that D2 is a useful tool to study MAP kinase function(s) during oocyte maturation. Truncated substrates such as D2, which constitutively interact with MAP kinases, may also be helpful to study signal transduction by MAP kinases in other cellular processes.

Germinal vesicle material is dispensable for oscillations in cdc2 and MAP kinase activities, cyclin B degradation and synthesis during meiosis in Xenopus oocytes

1998 ◽  
Vol 90 (6-7) ◽  
pp. 497-508 ◽  
Author(s):  
Daniel Fisher ◽  
Olivier Coux ◽  
Guillaume Bompard-Maréchal ◽  
Marcel Dorée
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Germinal Vesicle ◽  
Cyclin B

scholarly journals Mitogen-activated protein kinase activation down-regulates a mechanism that inactivates cyclin B-cdc2 kinase in G2-arrested oocytes.

1997 ◽  
Vol 8 (2) ◽  
pp. 249-261 ◽  
Author(s):  
A Abrieu ◽  
M Dorée ◽  
A Picard
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Cyclin B ◽  
Mitogen Activated Protein Kinase ◽  
Cdc2 Kinase ◽  
Hormonal Stimulation ◽  
Germinal Vesicle Breakdown ◽  
Kinase Activation ◽  
Map Kinase Phosphatase ◽  
Mitogen Activated Protein

The G2 arrest of oocytes from frogs, clams, and starfish requires that preformed cyclin B-cdc2 complexes [prematuration-promoting factor (MPF)] be kept in an inactive form that is largely due to inhibitory phosphorylation of this pre-MPF. We have investigated the role of mitogen-activated protein (MAP) kinase in the activation of this pre-MPF. The cytoplasm of both frog and starfish oocytes contains an activity that can rapidly inactivate injected MPF. When the MAP kinase of G2-arrested starfish or Xenopus oocytes was prematurely activated by microinjection of c-mos or Ste-11 delta N fusion proteins, the rate and extent of MPF inactivation was much reduced. Both effects were suppressed by expression of the specific MAP kinase phosphatase Pyst 1. These results show that MAP kinase down-regulates a mechanism that inactivates cyclin B-cdc2 kinase in Xenopus oocytes. In starfish oocytes, however, MAP kinase activation occurs only after germinal vesicle breakdown, much after MPF activation. In this case, down-regulation of the cyclin B-cdc2 inhibiting pathway is a sensitive response to hormonal stimulation that does not require MAP kinase activation.

Role of phosphatidylinositide metabolism in ras-induced Xenopus oocyte maturation

1990 ◽  
Vol 10 (3) ◽  
pp. 923-929
Author(s):  
B T Pan ◽  
G M Cooper
Keyword(s):  
Xenopus Oocytes ◽  
Second Messengers ◽  
Phospholipid Metabolism ◽  
Meiotic Maturation ◽  
Ras Oncogene ◽  
Ras Protein ◽  
32P Incorporation ◽  
Kinetics Of ◽  
Oncogene Protein

Microinjection of Xenopus oocytes with ras protein (p21) was used to investigate the role of phospholipid metabolism in ras-induced meiotic maturation. Induction of meiosis by ras was compared with induction by progesterone, insulin, and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA). Neomycin, which specifically binds to phosphatidylinositides and inhibits their metabolism, blocked meiotic maturation induced by ras or insulin but not by progesterone or TPA. In addition, p21 and TPA, but not insulin or progesterone, stimulated the incorporation of 32Pi into oocyte lipids. ras protein specifically stimulated 32P incorporation into phosphatidylinositides, whereas both ras and TPA stimulated 32P incorporation into phosphatidylcholine and phosphatidylethanolamine. The stimulatory effect of p21 on phosphatidylinositide metabolism correlated with the dose response and kinetics of ras-induced meiotic maturation. In addition, the ras oncogene protein was more potent than the proto-oncogene protein both in inducing meiotic maturation and in stimulating phosphatidylinositide metabolism. These results indicate that phosphatidylinositide turnover is required for ras-induced meiosis and suggest that phosphatidylinositide-derived second messengers mediate the biological activity of ras in Xenopus oocytes.

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
Keyword(s):  
Cell Cycle ◽  
Map Kinase ◽  
Cell Cycle Progression ◽  
Mitotic Cell ◽  
Model Systems ◽  
Cyclin B ◽  
Cdc2 Kinase ◽  
Meiotic Chromosomes ◽  
Map Kinase Cascade ◽  
Kinase Cascade

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.

scholarly journals Cyclin B in Xenopus oocytes: implications for the mechanism of pre-MPF activation.

1991 ◽  
Vol 10 (1) ◽  
pp. 177-182 ◽  
Author(s):  
J. Gautier ◽  
J. L. Maller
Keyword(s):  
Xenopus Oocytes ◽  
Cyclin B
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