Centralspindlin Recruits ALIX to the Midbody during Cytokinetic Abscission in Drosophila via a Mechanism Analogous to Virus Budding.
ALIX
CEP55
ESCRT-III
L-domain
LxxLF motif
Pavarotti
TSG101
abscission
centralspindlin
cytokinesis
Journal
Current biology : CB
ISSN: 1879-0445
Titre abrégé: Curr Biol
Pays: England
ID NLM: 9107782
Informations de publication
Date de publication:
21 10 2019
21 10 2019
Historique:
received:
07
12
2018
revised:
06
07
2019
accepted:
11
09
2019
pubmed:
15
10
2019
medline:
22
8
2020
entrez:
15
10
2019
Statut:
ppublish
Résumé
Abscission, the final step of cytokinesis, cleaves the thin intercellular bridge connecting the two daughter cells [1-6]. The scaffold protein ALIX is a core component of the abscission machinery with an evolutionarily conserved role in midbody recruitment of ESCRT-III [7-11], which mediates the final cut [1-5, 8-10, 12-14]. In mammalian cells, the centralspindlin complex recruits the major midbody organizer CEP55 that directly binds and recruits ALIX and ESCRT-I [7-9, 15-17], which in turn cooperatively recruit ESCRT-III [8, 9, 18]. However, CEP55 is missing in Drosophila melanogaster and other invertebrates [6, 9, 19], and it is unknown how the abscission machinery is recruited to the midbody in the absence of CEP55. Here, we address how Drosophila ALIX is recruited to the midbody. Surprisingly, ALIX localizes to the midbody via its V-domain, independently of the GPPX
Identifiants
pubmed: 31607533
pii: S0960-9822(19)31187-X
doi: 10.1016/j.cub.2019.09.025
pii:
doi:
Substances chimiques
ALIX protein, Drosophila
0
Drosophila Proteins
0
Microfilament Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3538-3548.e7Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.