Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes
<jats:p>Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in synchronized sea star oocytes from prophase...
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications, Ltd
2022
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| Online Access: | https://hdl.handle.net/1721.1/146773 |
| _version_ | 1811086610418106368 |
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| author | Swartz, S Zachary Nguyen, Hieu T McEwan, Brennan C Adamo, Mark E Cheeseman, Iain M Kettenbach, Arminja N |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Swartz, S Zachary Nguyen, Hieu T McEwan, Brennan C Adamo, Mark E Cheeseman, Iain M Kettenbach, Arminja N |
| author_sort | Swartz, S Zachary |
| collection | MIT |
| description | <jats:p>Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in synchronized sea star oocytes from prophase I through the first embryonic cleavage. Although we found that protein levels were broadly stable, our analysis reveals that dynamic waves of phosphorylation underlie each meiotic stage. We found that the phosphatase PP2A-B55 is reactivated at the meiosis I/meiosis II (MI/MII) transition, resulting in the preferential dephosphorylation of threonine residues. Selective dephosphorylation is critical for directing the MI/MII transition as altering PP2A-B55 substrate preferences disrupts key cell cycle events after MI. In addition, threonine to serine substitution of a conserved phosphorylation site in the substrate INCENP prevents its relocalization at anaphase I. Thus, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.</jats:p> |
| first_indexed | 2024-09-23T13:28:59Z |
| format | Article |
| id | mit-1721.1/146773 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T13:28:59Z |
| publishDate | 2022 |
| publisher | eLife Sciences Publications, Ltd |
| record_format | dspace |
| spelling | mit-1721.1/1467732022-12-08T03:21:16Z Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes Swartz, S Zachary Nguyen, Hieu T McEwan, Brennan C Adamo, Mark E Cheeseman, Iain M Kettenbach, Arminja N Massachusetts Institute of Technology. Department of Biology <jats:p>Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in synchronized sea star oocytes from prophase I through the first embryonic cleavage. Although we found that protein levels were broadly stable, our analysis reveals that dynamic waves of phosphorylation underlie each meiotic stage. We found that the phosphatase PP2A-B55 is reactivated at the meiosis I/meiosis II (MI/MII) transition, resulting in the preferential dephosphorylation of threonine residues. Selective dephosphorylation is critical for directing the MI/MII transition as altering PP2A-B55 substrate preferences disrupts key cell cycle events after MI. In addition, threonine to serine substitution of a conserved phosphorylation site in the substrate INCENP prevents its relocalization at anaphase I. Thus, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.</jats:p> 2022-12-07T15:16:44Z 2022-12-07T15:16:44Z 2021 2022-12-07T15:08:31Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/146773 Swartz, S Zachary, Nguyen, Hieu T, McEwan, Brennan C, Adamo, Mark E, Cheeseman, Iain M et al. 2021. "Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes." eLife, 10. en 10.7554/ELIFE.70588 eLife Creative Commons Attribution 4.0 International license https://creativecommons.org/licenses/by/4.0/ application/pdf eLife Sciences Publications, Ltd eLife |
| spellingShingle | Swartz, S Zachary Nguyen, Hieu T McEwan, Brennan C Adamo, Mark E Cheeseman, Iain M Kettenbach, Arminja N Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title | Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title_full | Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title_fullStr | Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title_full_unstemmed | Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title_short | Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes |
| title_sort | selective dephosphorylation by pp2a b55 directs the meiosis i meiosis ii transition in oocytes |
| url | https://hdl.handle.net/1721.1/146773 |
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