Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes
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...
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2021-08-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/70588 |
id |
doaj-f633bbf5007145098af78b2bf58abe6b |
---|---|
record_format |
Article |
spelling |
doaj-f633bbf5007145098af78b2bf58abe6b2021-08-17T11:22:02ZengeLife Sciences Publications LtdeLife2050-084X2021-08-011010.7554/eLife.70588Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytesS Zachary Swartz0https://orcid.org/0000-0002-3264-6880Hieu T Nguyen1Brennan C McEwan2Mark E Adamo3Iain M Cheeseman4https://orcid.org/0000-0002-3829-5612Arminja N Kettenbach5https://orcid.org/0000-0003-3979-4576Whitehead Institute for Biomedical Research, Cambridge, United States; Department of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, United StatesDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, United StatesNorris Cotton Cancer Center, Geisel School of Medicine at Dartmouth, Lebanon, United StatesWhitehead Institute for Biomedical Research, Cambridge, United States; Department of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, United States; Norris Cotton Cancer Center, Geisel School of Medicine at Dartmouth, Lebanon, United StatesMeiosis 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.https://elifesciences.org/articles/70588meiosispatiria miniataphosphatasesproteomics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
S Zachary Swartz Hieu T Nguyen Brennan C McEwan Mark E Adamo Iain M Cheeseman Arminja N Kettenbach |
spellingShingle |
S Zachary Swartz Hieu T Nguyen Brennan C McEwan Mark E Adamo Iain M Cheeseman Arminja N Kettenbach Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes eLife meiosis patiria miniata phosphatases proteomics |
author_facet |
S Zachary Swartz Hieu T Nguyen Brennan C McEwan Mark E Adamo Iain M Cheeseman Arminja N Kettenbach |
author_sort |
S Zachary Swartz |
title |
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_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_sort |
selective dephosphorylation by pp2a-b55 directs the meiosis i-meiosis ii transition in oocytes |
publisher |
eLife Sciences Publications Ltd |
series |
eLife |
issn |
2050-084X |
publishDate |
2021-08-01 |
description |
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. |
topic |
meiosis patiria miniata phosphatases proteomics |
url |
https://elifesciences.org/articles/70588 |
work_keys_str_mv |
AT szacharyswartz selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes AT hieutnguyen selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes AT brennancmcewan selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes AT markeadamo selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes AT iainmcheeseman selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes AT arminjankettenbach selectivedephosphorylationbypp2ab55directsthemeiosisimeiosisiitransitioninoocytes |
_version_ |
1721205150544035840 |