Phosphorylation of ELYS promotes its interaction with VAPB at decondensing chromosomes during mitosis.
ELYS
FFAT-motif
Mitosis
Nuclear Envelope
VAPB
Journal
EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049
Informations de publication
Date de publication:
11 Apr 2024
11 Apr 2024
Historique:
received:
15
09
2023
accepted:
11
03
2024
revised:
23
02
2024
medline:
12
4
2024
pubmed:
12
4
2024
entrez:
11
4
2024
Statut:
aheadofprint
Résumé
ELYS is a nucleoporin that localizes to the nuclear side of the nuclear pore complex (NPC) in interphase cells. In mitosis, it serves as an assembly platform that interacts with chromatin and then with nucleoporin subcomplexes to initiate post-mitotic NPC assembly. Here we identify ELYS as a major binding partner of the membrane protein VAPB during mitosis. In mitosis, ELYS becomes phosphorylated at many sites, including a predicted FFAT (two phenylalanines in an acidic tract) motif, which mediates interaction with the MSP (major sperm protein)-domain of VAPB. Binding assays using recombinant proteins or cell lysates and co-immunoprecipitation experiments show that VAPB binds the FFAT motif of ELYS in a phosphorylation-dependent manner. In anaphase, the two proteins co-localize to the non-core region of the newly forming nuclear envelope. Depletion of VAPB results in prolonged mitosis, slow progression from meta- to anaphase and in chromosome segregation defects. Together, our results suggest a role of VAPB in mitosis upon recruitment to or release from ELYS at the non-core region of the chromatin in a phosphorylation-dependent manner.
Identifiants
pubmed: 38605278
doi: 10.1038/s44319-024-00125-6
pii: 10.1038/s44319-024-00125-6
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft (DFG)
ID : SFB1190,P07
Organisme : Deutsche Forschungsgemeinschaft (DFG)
ID : SFB1190,Z02
Informations de copyright
© 2024. The Author(s).
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