Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly in Drosophila

Author:

Emond-Fraser Virginie12,Larouche Myreille12,Kubiniok Peter1,Bonneil Éric1,Li Jingjing1,Bourouh Mohammed1,Frizzi Laura12,Thibault Pierre13,Archambault Vincent12ORCID

Affiliation:

1. Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, H3T 1J4, Quebec, Canada

2. Département de biochimie et médecine moléculaire, Université de Montréal, Montréal, H3T 1J4, Quebec, Canada

3. Département de chimie, Université de Montréal, Montréal, H3T 1J4, Quebec, Canada

Abstract

Mitotic exit requires the dephosphorylation of many proteins whose phosphorylation was needed for mitosis. Protein phosphatase 2A with its B55 regulatory subunit (PP2A-B55) promotes this transition. However, the events and substrates that it regulates are incompletely understood. We used proteomic approaches in Drosophila to identify proteins that interact with and are dephosphorylated by PP2A-B55. Among several candidates, we identified emerin (otefin in Drosophila ). Emerin resides in the inner nuclear membrane and interacts with the DNA-binding protein barrier-to-autointegration factor (BAF) via a LEM domain. We found that the phosphorylation of emerin at Ser50 and Ser54 near its LEM domain negatively regulates its association with BAF, lamin and additional emerin in mitosis. We show that dephosphorylation of emerin at these sites by PP2A-B55 determines the timing of nuclear envelope reformation. Genetic experiments indicate that this regulation is required during embryonic development. Phosphoregulation of the emerin–BAF complex formation by PP2A-B55 appears as a key event of mitotic exit that is likely conserved across species.

Funder

Fonds de Recherche du Québec – Santé

CIHR

Fonds de recherche du Québec – Nature et technologies

Publisher

The Royal Society

Subject

General Biochemistry, Genetics and Molecular Biology,Immunology,General Neuroscience

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