ESCRT-III/Vps4 Controls Heterochromatin-Nuclear Envelope Attachments.
Chromatin
/ metabolism
Endosomal Sorting Complexes Required for Transport
/ metabolism
Heterochromatin
/ metabolism
Membrane Proteins
/ metabolism
Mitosis
/ physiology
Nuclear Envelope
/ metabolism
Nuclear Proteins
/ metabolism
Schizosaccharomyces
/ metabolism
Schizosaccharomyces pombe Proteins
/ metabolism
ESCRT-III
Lem2
Vps4
fission yeast
heterochromatin
nuclear envelope
Journal
Developmental cell
ISSN: 1878-1551
Titre abrégé: Dev Cell
Pays: United States
ID NLM: 101120028
Informations de publication
Date de publication:
06 04 2020
06 04 2020
Historique:
received:
24
04
2019
revised:
05
12
2019
accepted:
27
01
2020
pubmed:
29
2
2020
medline:
24
10
2020
entrez:
29
2
2020
Statut:
ppublish
Résumé
Eukaryotic genomes are organized within the nucleus through interactions with inner nuclear membrane (INM) proteins. How chromatin tethering to the INM is controlled in interphase and how this process contributes to subsequent mitotic nuclear envelope (NE) remodeling remains unclear. We have probed these fundamental questions using the fission yeast Schizosaccharomyces japonicus, which breaks and reforms the NE during mitosis. We show that attachments between heterochromatin and the transmembrane Lem2-Nur1 complex at the INM are remodeled in interphase by the ESCRT-III/Vps4 machinery. Failure of ESCRT-III/Vps4 to release Lem2-Nur1 from heterochromatin leads to persistent association of chromosomes with the INM throughout mitosis. At mitotic exit, such trapping of Lem2-Nur1 on heterochromatin prevents it from re-establishing nucleocytoplasmic compartmentalization. Our work identifies the Lem2-Nur1 complex as a substrate for the nuclear ESCRT machinery and explains how the dynamic tethering of chromosomes to the INM is linked to the establishment of nuclear compartmentalization.
Identifiants
pubmed: 32109380
pii: S1534-5807(20)30060-5
doi: 10.1016/j.devcel.2020.01.028
pmc: PMC7139201
mid: EMS85884
pii:
doi:
Substances chimiques
Chromatin
0
Endosomal Sorting Complexes Required for Transport
0
Heterochromatin
0
Membrane Proteins
0
Nuclear Proteins
0
Schizosaccharomyces pombe Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
27-41.e6Subventions
Organisme : Wellcome Trust
ID : 103741
Pays : United Kingdom
Organisme : Cancer Research UK
ID : FC001002
Pays : United Kingdom
Organisme : Medical Research Council
ID : FC001002
Pays : United Kingdom
Organisme : Wellcome Trust
ID : FC001002
Pays : United Kingdom
Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.
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