Par complex cluster formation mediated by phase separation.
Animals
COS Cells
Cell Cycle
Cell Differentiation
Cell Survival
Chlorocebus aethiops
Drosophila Proteins
/ chemistry
Drosophila melanogaster
/ cytology
Green Fluorescent Proteins
/ metabolism
HEK293 Cells
Humans
Larva
/ cytology
Multiprotein Complexes
/ chemistry
Neurons
/ cytology
Protein Domains
Protein Kinase C
/ metabolism
Rats
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
08 05 2020
08 05 2020
Historique:
received:
28
07
2019
accepted:
16
04
2020
entrez:
10
5
2020
pubmed:
10
5
2020
medline:
6
8
2020
Statut:
epublish
Résumé
The evolutionarily conserved Par3/Par6/aPKC complex regulates the polarity establishment of diverse cell types and distinct polarity-driven functions. However, how the Par complex is concentrated beneath the membrane to initiate cell polarization remains unclear. Here we show that the Par complex exhibits cell cycle-dependent condensation in Drosophila neuroblasts, driven by liquid-liquid phase separation. The open conformation of Par3 undergoes autonomous phase separation likely due to its NTD-mediated oligomerization. Par6, via C-terminal tail binding to Par3 PDZ3, can be enriched to Par3 condensates and in return dramatically promote Par3 phase separation. aPKC can also be concentrated to the Par3N/Par6 condensates as a client. Interestingly, activated aPKC can disperse the Par3/Par6 condensates via phosphorylation of Par3. Perturbations of Par3/Par6 phase separation impair the establishment of apical-basal polarity during neuroblast asymmetric divisions and lead to defective lineage development. We propose that phase separation may be a common mechanism for localized cortical condensation of cell polarity complexes.
Identifiants
pubmed: 32385244
doi: 10.1038/s41467-020-16135-6
pii: 10.1038/s41467-020-16135-6
pmc: PMC7211019
doi:
Substances chimiques
Drosophila Proteins
0
Multiprotein Complexes
0
Green Fluorescent Proteins
147336-22-9
Protein Kinase C
EC 2.7.11.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2266Références
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