Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization.


Journal

The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356

Informations de publication

Date de publication:
06 02 2023
Historique:
received: 15 04 2022
revised: 12 09 2022
accepted: 05 11 2022
entrez: 14 12 2022
pubmed: 15 12 2022
medline: 17 12 2022
Statut: ppublish

Résumé

Nuclear pore complexes (NPCs) are large proteinaceous assemblies that mediate nuclear compartmentalization. NPCs undergo large-scale structural rearrangements during mitosis in metazoans and some fungi. However, our understanding of NPC remodeling beyond mitosis remains limited. Using time-lapse fluorescence microscopy, we discovered that NPCs undergo two mechanistically separable remodeling events during budding yeast meiosis in which parts or all of the nuclear basket transiently dissociate from the NPC core during meiosis I and II, respectively. Meiosis I detachment, observed for Nup60 and Nup2, is driven by Polo kinase-mediated phosphorylation of Nup60 at its interface with the Y-complex. Subsequent reattachment of Nup60-Nup2 to the NPC core is facilitated by a lipid-binding amphipathic helix in Nup60. Preventing Nup60-Nup2 reattachment causes misorganization of the entire nuclear basket in gametes. Strikingly, meiotic nuclear basket remodeling also occurs in the distantly related fission yeast, Schizosaccharomyces pombe. Our study reveals a conserved and developmentally programmed aspect of NPC plasticity, providing key mechanistic insights into the nuclear basket organization.

Identifiants

pubmed: 36515990
pii: 213751
doi: 10.1083/jcb.202204039
pmc: PMC9754704
pii:
doi:

Substances chimiques

Nuclear Pore Complex Proteins 0
Nup60 protein, S cerevisiae 0
NUP2 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIA NIH HHS
ID : DP2 AG055946
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007232
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG071801
Pays : United States
Organisme : European Research Council
ID : 670821
Pays : International
Organisme : NIH HHS
ID : R01AG071801
Pays : United States

Commentaires et corrections

Type : CommentIn

Informations de copyright

© 2022 King et al.

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Auteurs

Grant A King (GA)

Department of Molecular and Cell Biology, University of California, Berkeley, CA.

Rahel Wettstein (R)

Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Max Perutz Labs, University of Vienna, Vienna, Austria.

Joseph M Varberg (JM)

Stowers Institute for Medical Research, Kansas City, MO.

Keerthana Chetlapalli (K)

Department of Molecular and Cell Biology, University of California, Berkeley, CA.

Madison E Walsh (ME)

Department of Molecular and Cell Biology, University of California, Berkeley, CA.

Ludovic C J Gillet (LCJ)

Institute of Molecular Systems Biology, Department of Biology, ETH Zürich, Zürich, Switzerland.

Claudia Hernández-Armenta (C)

European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Cambridge, UK.

Pedro Beltrao (P)

Institute of Molecular Systems Biology, Department of Biology, ETH Zürich, Zürich, Switzerland.
European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Cambridge, UK.

Ruedi Aebersold (R)

Institute of Molecular Systems Biology, Department of Biology, ETH Zürich, Zürich, Switzerland.

Sue L Jaspersen (SL)

Stowers Institute for Medical Research, Kansas City, MO.
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS.

Joao Matos (J)

Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Max Perutz Labs, University of Vienna, Vienna, Austria.

Elçin Ünal (E)

Department of Molecular and Cell Biology, University of California, Berkeley, CA.

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Classifications MeSH