ArticleThe EMBO journal1992
The 'second-codon rule' and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 144 citations in OpenAlex.
- Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes.The Journal of reproduction and development · 2018Article
- Maternal Wnt/STOP signaling promotes cell division during early Xenopus embryogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mos in the oocyte: how to use MAPK independently of growth factors and transcription to control meiotic divisions.Journal of signal transduction · 2011Article
- Kicked by Mos and tuned by MPF-the initiation of the MAPK cascade in Xenopus oocytes.HFSP journal · 2009Article
- Mechanistic studies of the mitotic activation of Mos.Molecular and cellular biology · 2006Article
- The status of human nuclear transfer.Stem cell reviews · 2006Review
- Control of protein life-span by N-terminal methionine excision.The EMBO journal · 2003Article
- Dissection of c-MOS degron.The EMBO journal · 2002Article
- Cyclin B/cdc2 induces c-Mos stability by direct phosphorylation in Xenopus oocytes.Molecular biology of the cell · 2001Article
- c-Mos forces the mitotic cell cycle to undergo meiosis II to produce haploid gametes.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Residual Cdc2 activity remaining at meiosis I exit is essential for meiotic M-M transition in Xenopus oocyte extracts.The EMBO journal · 2000Article
- Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes.The EMBO journal · 2000Article
- c-mos and cdc2 cooperate in the translational activation of fibroblast growth factor receptor-1 during Xenopus oocyte maturation.Molecular biology of the cell · 1999Article
- Evidence for an important role of serine 16 and its phosphorylation in the stabilization of c-Mos.Oncogene · 1999Article
- Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association.Oncogene · 1999Article
- Proteasome activity is required for anthrax lethal toxin to kill macrophages.Infection and immunity · 1999Article
- The ubiquitin-proteasome pathway: on protein death and cell life.The EMBO journal · 1998Review
- The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway.The EMBO journal · 1998Article
- Meiotic maturation in Xenopus requires polyadenylation of multiple mRNAs.The EMBO journal · 1998Article
- The beta subunit of CKII negatively regulates Xenopus oocyte maturation.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The c-mos proto-oncogene product, Mos, functions in both early (germinal vesicle breakdown) and late (metaphase II arrest) steps during meiotic maturation in Xenopus oocytes. In the early step, Mos is only partially phosphorylated and metabolically unstable, while in the late step it is fully phosphorylated and highly stable. Using a number of Mos mutants expressed in oocytes, we show here that the instability of Mos in the early step is determined primarily by its penultimate N-terminal residue, or by a rule referred to here as the 'second-codon rule'. We demonstrate that unstable Mos is degraded by the ubiquitin-dependent pathway. In the late step, on the other hand, Mos is stabilized by autophosphorylation at Ser3, which probably acts to prevent the N-terminus of Mos from being recognized by a ubiquitin-protein ligase. Moreover, we show that Ser3 phosphorylation is essential for Mos to exert its full cytostatic factor (CSF) activity in fully mature oocytes. Thus, a few N-terminal amino acids are primary determinants of both the metabolic stability and physiological activity of Mos during the meiotic cell cycle.
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