Cited by 25Reproductive Biology and FertilityRNA Research and SplicingReproductive biology and impacts on aquatic species

Possible Involvement of Nemo-like Kinase 1 in Xenopus Oocyte Maturation As a Kinase Responsible for Pumilio1, Pumilio2, and CPEB Phosphorylation

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Ota, Ryoma, Kotani, Tomoya, Yamashita, Masakane·2011·Biochemistry

Abstract

Members of the mitogen-activated protein kinase (MAPK) family play important roles in Xenopus oocyte maturation. Nemo-like kinase (NLK), an atypical MAPK, is known to function in multiple developmental processes in vertebrates and invertebrates, but its involvement in gametogenesis and gamete maturation is unknown. In this study, we biochemically examined NLK1 during Xenopus oocyte maturation. NLK1 is expressed in immature oocytes, and its protein level remains constant during maturation. NLK1 is inactive in immature oocytes but is activated during maturation, depending on Mos protein synthesis but not on p42 MAPK activation. Overexpression of NLK1 by injection of 5 ng of mRNA accelerates progesterone-induced oocyte maturation by enhancing Cyclin B1 protein synthesis through the translational activation of its mRNA, in accordance with precocious phosphorylation of Pumilio1 (Pum1), Pumilio2 (Pum2), and cytoplasmic polyadenylation element-binding protein (CPEB), key regulators of the translational control of mRNAs stored in oocytes. A higher level of NLK1 expression by injection of 50 ng of mRNA induces Pum1/Pum2/CPEB phosphorylation, CPEB degradation, Cyclin B1 protein synthesis, and oocyte maturation in the absence of progesterone. NLK1 phosphorylates Pum1, Pum2, and CPEB in vitro. These findings provide the first evidence for the involvement of NLK1 in Xenopus oocyte maturation. We suggest that NLK1 acts as a kinase downstream of Mos and catalyzes phosphorylation of Pum1, Pu…

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Crossref · 10.1021/bi2002696

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  • NLK was initially shown to be involved in various developmental processes, such as promotion of mesoderm specification in sea urchins, mesoderm patterning, patterning of midbrain and forebrain in zebrafish, and oocyte maturation in Xenopus Laevis and in mouse testes.

    “NLK was initially shown to be involved in various developmental processes, such as the promotion of mesoderm specification in sea urchins [32], mesoderm patterning, patterning of midbrain and forebrain in zebrafish [33], as well as oocyte maturation in Xenopus Laevis [34] and in mouse testes [35].”

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Authors
Ota, R., Kotani, T., & Yamashita, M.
Affiliations
Hokkaido University (JP)
Corresponding author
Yamashita, Masakane
Venue
Biochemistry
Published
2011-06-04
Volume
50
Issue
25
Pages
5648-5659
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2323212920
Cited by
25
References
2
Citations by year
2023: 1 · 2021: 2 · 2020: 3 · 2018: 5 · 2017: 2 · 2016: 1 · 2015: 2 · 2013: 3 · 2012: 6
FWCI
2.83
Type
journal article
Language
en
Open access
Licence
cc-by-nc-nd
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
Funders
Japan Society for the Promotion of Science (23013001, 23770196, 23370027)
Topics
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Reproductive biology and impacts on aquatic species
Keywords
oocyte maturation, CPEB, protein phosphorylation, cyclin B1, translational regulation, mRNA storage, progesterone, Xenopus oocytes, kinase activity
MeSH terms
Animals, Catalysis, Oocytes, Oogenesis, Phosphorylation, RNA, Messenger, Transcription Factors, Protein Biosynthesis, Xenopus laevis, RNA-Binding Proteins, Mitogen-Activated Protein Kinases, Xenopus Proteins, mRNA Cleavage and Polyadenylation Factors, Cyclin B1

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