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  Histone H3 phosphorylation during Xenopus oocyte maturation: Regulation by the MAP kinase/p90Rsk pathway and uncoupling from DNA condensation.

Schmitt, A., Gutierrez, G. J., Lenart, P., Ellenberg, J., & Nebreda, A. R. (2002). Histone H3 phosphorylation during Xenopus oocyte maturation: Regulation by the MAP kinase/p90Rsk pathway and uncoupling from DNA condensation. FEBS Letters, 518(1-13), 23-28. doi:10.1016/S0014-5793(02)02630-3.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-129E-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-12A3-1
Genre: Journal Article

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2642148.pdf (Publisher version), 465KB
 
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Schmitt, A., Author
Gutierrez, G. J., Author
Lenart, P.1, Author              
Ellenberg, J., Author
Nebreda, A. R., Author
Affiliations:
1Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society, ou_2640691              

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 Abstract: Here we show that during the meiotic maturation of Xenopus oocytes, histone H3 becomes phosphorylated on serine-10 at about the time of maturation promoting factor activation and meiosis I entry. However, overexpression of cAMP-dependent protein kinase that blocks entry into M phase, also leads to massive serine-10 phosphorylation of histone H3 in intact Xenopus oocytes but does not cause chromosome condensation. We also show that the phosphorylation of histone H3 during oocyte maturation requires the activation of the mitogen-activated protein kinase/p90Rsk pathway. Our results indicate that in G2-arrested oocytes, which are about to enter M phase, histone H3 phosphorylation is not sufficient for chromosome condensation.

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Language(s): eng - English
 Dates: 2002-04-052002-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/S0014-5793(02)02630-3
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 518 (1-13) Sequence Number: - Start / End Page: 23 - 28 Identifier: -