MassIVE MSV000085949

Complete Public PXD020916

Selective dephosphorylation by PP2A-B55 directs the meiosis I - meiosis II transition in oocytes

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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 sea star oocytes from prophase I through the first embryonic cleavage. Although protein levels are broadly stable, dynamic waves of phosphorylation underlie each meiotic stage. We find that the phosphatase PP2A-B55 is reactivated at the Meiosis I/II 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 meiosis I. 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. [doi:10.25345/C54T9F] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: starfish ; sea star ; gamete ; meiosis ; oocyte ; prophase ; PP1 ; PP2A ; PP2A-B55 ; protein phosphatase ; phosphorylation ; dephosphorylation ; INCENP ; TMT

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Principal Investigators:
(in alphabetical order) 		Arminja Kettenbach, The Geisel School of Medicine at Dartmouth, United States
Submitting User: madamo
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