Article abstract
Nature Cell Biology 8, 1084 - 1094 (2006)
Published online: 10 September 2006 | doi:10.1038/ncb1472
Meiotic regulation of the CDK activator RINGO/Speedy by ubiquitin-proteasome-mediated processing and degradation
Gustavo J. Gutierrez1,2, Andrea Vögtlin1,3, Ana Castro4, Ingvar Ferby1,5, Giorgia Salvagiotto1,6, Ze'ev Ronai2, Thierry Lorca4 & Angel R. Nebreda1,7
Abstract
Xenopus RINGO/Speedy (XRINGO) is a potent inducer of oocyte meiotic maturation that can directly activate Cdk1 and Cdk2. Here, we show that endogenous XRINGO protein accumulates transiently during meiosis I entry and then is downregulated. This tight regulation of XRINGO expression is the consequence of two interconnected mechanisms: processing and degradation. XRINGO processing involves recognition of at least three distinct phosphorylated recognition motifs by the SCF
TrCP ubiquitin ligase, followed by proteasome-mediated limited degradation, resulting in an amino-terminal XRINGO fragment. XRINGO processing is directly stimulated by several kinases, including protein kinase A and glycogen synthase kinase-3
, and may contribute to the maintenance of G2 arrest. On the other hand, XRINGO degradation after meiosis I is mediated by the ubiquitin ligase Siah-2, which probably requires phosphorylation of XRINGO on Ser 243 and may be important for the omission of S phase at the meiosis-I–meiosis-II transition in Xenopus oocytes.
- EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
- BIMR, 10901 N. Torrey Pines Road, La Jolla, CA 92037, USA.
- Institute of Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland.
- CRBM-CNRS, 1919 Route de Mende, 34096 Montpellier, France.
- Max-Planck Institute of Neurobiology, Am Klopferspitz 18, 82152 Martinsried, Germany.
- IMP, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
- CNIO (Spanish National Cancer Center), Melchor Fernandez Almagro, 3, E-28029 Madrid, Spain.
Correspondence to: e-mail: anebreda@cnio.es
Correspondence to: Gustavo J. Gutierrez1,2Angel R. Nebreda1,7 e-mail: gustavo@burnham.org
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
RESEARCH
Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradationNature Letters to Editor (13 Oct 2005)
Functional interaction between p90 Rsk2 and Emi1 contributes to the metaphase arrest of mouse oocytesThe EMBO Journal Article (24 Nov 2004)
Emi1 is required for cytostatic factor arrest in vertebrate eggsNature Letters to Editor (25 Apr 2002)
Phosphorylation of Erp1 by p90rsk is required for cytostatic factor arrest in Xenopus laevis eggsNature Letters to Editor (26 Apr 2007)
See all 23 matches for Research
