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Updated: Jul 25, 2026

Xenopus laevis as a Model to Identify Translation Impairment
Published on: September 27, 2015
The pathway of MAP kinase mediation of CSF arrest in Xenopus oocytes
J L Maller1, M S Schwab, B T Roberts
1Howard Hughes Medical Institute and Department of Pharmacology, University of Colorado School of Medicine, Denver 80262, USA. Jim.Maller@uchsc.edu
Abstract:
A cytoplasmic activity in mature oocytes responsible for second meiotic metaphase arrest was identified over 30 years ago in amphibian oocytes. In Xenopus oocytes CSF activity is initiated by the progesterone-dependent synthesis of Mos, a MAPK kinase kinase, which activates the MAPK pathway. CSF arrest is mediated by a sole MAPK target, the protein kinase p90Rsk which leads to inhibition of cyclin B degradation by the anaphase-promoting complex. Rsk phosphorylates and activates the Bub1 protein kinase, which may cause metaphase arrest due to inhibition of the anaphase-promoting complex (APC) by a conserved mechanism defined genetically in yeast and mammalian cells. CSF arrest in vertebrate oocytes by p90Rsk provides a potential link between the MAPK pathway and the spindle assembly checkpoint in the cell cycle.
Insights
Cytostatic factor (CSF) activity in oocytes, crucial for metaphase arrest, is initiated by Mos and the MAPK pathway. This process involves p90Rsk protein kinase, linking MAPK signaling to the spindle assembly checkpoint.
Area of Science:
- Cell Biology
- Molecular Biology
- Developmental Biology
Background:
- A cytoplasmic activity, known as cytostatic factor (CSF), causes metaphase arrest in mature oocytes.
- This arrest is essential for proper meiotic progression and has been studied for over 30 years in amphibians.
Purpose of the Study:
- To elucidate the molecular mechanisms underlying CSF-mediated metaphase arrest in Xenopus oocytes.
- To identify the key signaling pathways and protein interactions involved in maintaining meiotic arrest.
Main Methods:
- Investigated the role of the Mos-MAPK pathway in initiating CSF activity.
- Examined the function of p90Rsk, a MAPK target, in regulating cyclin B degradation.
- Assessed the phosphorylation and activation of Bub1 protein kinase by p90Rsk.
Main Results:
- Progesterone induces Mos synthesis, activating the MAPK pathway, which is upstream of CSF activity.
- p90Rsk directly inhibits cyclin B degradation by the anaphase-promoting complex (APC).
- p90Rsk phosphorylates and activates Bub1, a key component of the spindle assembly checkpoint.
Conclusions:
- CSF arrest in Xenopus oocytes is mediated by p90Rsk, a downstream target of the MAPK pathway.
- p90Rsk links MAPK signaling to the APC, preventing premature anaphase.
- This study reveals a conserved mechanism connecting the MAPK pathway and the spindle assembly checkpoint in cell cycle regulation.
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