Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
J Cell Biol April 25, 2005; 169 (2): 227-31.

p90Rsk is not involved in cytostatic factor arrest in mouse oocytes.

Dumont J , Umbhauer M , Rassinier P , Hanauer A , Verlhac MH .

Vertebrate oocytes arrest in metaphase of the second meiotic division (MII), where they maintain a high cdc2/cyclin B activity and a stable, bipolar spindle because of cytostatic factor (CSF) activity. The Mos-MAPK pathway is essential for establishing CSF. Indeed, oocytes from the mos-/- strain do not arrest in MII and activate without fertilization, as do Xenopus laevis oocytes injected with morpholino oligonucleotides directed against Mos. In Xenopus oocytes, p90Rsk (ribosomal S6 kinase), a MAPK substrate, is the main mediator of CSF activity. We show here that this is not the case in mouse oocytes. The injection of constitutively active mutant forms of Rsk1 and Rsk2 does not induce a cell cycle arrest in two-cell mouse embryos. Moreover, these two mutant forms do not restore MII arrest after their injection into mos-/- oocytes. Eventually, oocytes from the triple Rsk (1, 2, 3) knockout present a normal CSF arrest. We demonstrate that p90Rsk is not involved in the MII arrest of mouse oocytes.

PubMed ID: 15837801
PMC ID: PMC2171868
Article link: J Cell Biol

Species referenced: Xenopus
Genes referenced: cdk1 gnao1 mapk1 mos rps6ka1 rps6ka3

Article Images: [+] show captions
References [+] :
Bhatt, The protein kinase p90 rsk as an essential mediator of cytostatic factor activity. 1999, Pubmed, Xenbase