Article ; Online: Regulation of oocyte maturation: Role of conserved ERK signaling.
Molecular reproduction and development
2022 Volume 89, Issue 9, Page(s) 353–374
Abstract: During oogenesis, oocytes arrest at meiotic prophase I to acquire competencies for resuming meiosis, fertilization, and early embryonic development. Following this arrested period, oocytes resume meiosis in response to species-specific hormones, a ... ...
Abstract | During oogenesis, oocytes arrest at meiotic prophase I to acquire competencies for resuming meiosis, fertilization, and early embryonic development. Following this arrested period, oocytes resume meiosis in response to species-specific hormones, a process known as oocyte maturation, that precedes ovulation and fertilization. Involvement of endocrine and autocrine/paracrine factors and signaling events during maintenance of prophase I arrest, and resumption of meiosis is an area of active research. Studies in vertebrate and invertebrate model organisms have delineated the molecular determinants and signaling pathways that regulate oocyte maturation. Cell cycle regulators, such as cyclin-dependent kinase (CDK1), polo-like kinase (PLK1), Wee1/Myt1 kinase, and the phosphatase CDC25 play conserved roles during meiotic resumption. Extracellular signal-regulated kinase (ERK), on the other hand, while activated during oocyte maturation in all species, regulates both species-specific, as well as conserved events among different organisms. In this review, we synthesize the general signaling mechanisms and focus on conserved and distinct functions of ERK signaling pathway during oocyte maturation in mammals, non-mammalian vertebrates, and invertebrates such as Drosophila and Caenorhabditis elegans. |
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MeSH term(s) | Animals ; Caenorhabditis elegans/metabolism ; Cyclin-Dependent Kinases/metabolism ; Drosophila ; Drosophila Proteins/metabolism ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Female ; Hormones/metabolism ; Mammals ; Meiosis ; Oocytes/metabolism ; Oogenesis/physiology ; Phosphoric Monoester Hydrolases/metabolism ; Protein Kinases/metabolism ; Signal Transduction/physiology |
Chemical Substances | Drosophila Proteins ; Hormones ; Protein Kinases (EC 2.7.-) ; Myt1 protein, Drosophila (EC 2.7.1.-) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) |
Language | English |
Publishing date | 2022-07-31 |
Publishing country | United States |
Document type | Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural |
ZDB-ID | 20321-x |
ISSN | 1098-2795 ; 1040-452X |
ISSN (online) | 1098-2795 |
ISSN | 1040-452X |
DOI | 10.1002/mrd.23637 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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