6JUE
The complex of PDZ and PBM
Summary for 6JUE
| Entry DOI | 10.2210/pdb6jue/pdb |
| Descriptor | Partitioning defective 3 homolog, THR-ILE-ILE-THR-LEU, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | pdz-binding motif peptide, complex, peptide binding protein |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 13108.64 |
| Authors | |
| Primary citation | Liu, 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: 32385244DOI: 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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