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6JUE

The complex of PDZ and PBM

Summary for 6JUE
Entry DOI10.2210/pdb6jue/pdb
DescriptorPartitioning defective 3 homolog, THR-ILE-ILE-THR-LEU, SULFATE ION, ... (4 entities in total)
Functional Keywordspdz-binding motif peptide, complex, peptide binding protein
Biological sourceRattus norvegicus (Rat)
More
Total number of polymer chains2
Total formula weight13108.64
Authors
Liu, Z. (deposition date: 2019-04-13, release date: 2020-04-22, Last modification date: 2023-11-22)
Primary citationLiu, Z.,Yang, Y.,Gu, A.,Xu, J.,Mao, Y.,Lu, H.,Hu, W.,Lei, Q.Y.,Li, Z.,Zhang, M.,Cai, Y.,Wen, W.
Par complex cluster formation mediated by phase separation.
Nat Commun, 11:2266-2266, 2020
Cited by
PubMed Abstract: 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.
PubMed: 32385244
DOI: 10.1038/s41467-020-16135-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.549 Å)
Structure validation

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