Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response

• Published in: Nature communications Vol. 10; no. 1; pp. 3759 - 18
• Main Authors: Yang, Yi, Willis, Thea L., Button, Robert W., Strang, Conor J., Fu, Yuhua, Wen, Xue, Grayson, Portia R. C., Evans, Tracey, Sipthorpe, Rebecca J., Roberts, Sheridan L., Hu, Bing, Zhang, Jianke, Lu, Boxun, Luo, Shouqing
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.08.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 13; 13/1; 13/106; 13/109; 13/2; 13/31; 13/51; 13/89; 14; 14/19; 631/45/470; 631/57/2269; 631/57/2272; 631/80/39/2346; 82/29; 82/51; 82/80; 82/83; Adaptor Proteins, Signal Transducing - genetics; Adaptor Proteins, Signal Transducing - metabolism; Animals; Autophagy; Autophagy - physiology; Cargo compartments; Cell Line; Co-Repressor Proteins; Condensation; Cytoplasm - metabolism; Daxx protein; Drosophila; Female; Gene Knockdown Techniques; HEK293 Cells; HeLa Cells; Humanities and Social Sciences; Humans; Intracellular; Kelch-Like ECH-Associated Protein 1 - metabolism; Liquid phases; Male; Mice; Molecular Chaperones; multidisciplinary; NF-E2-Related Factor 2 - metabolism; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Phagocytosis; Phase separation; Protein Binding; Protein Folding; Protein Interaction Domains and Motifs; Proteins; Quality control; RNA-Binding Proteins - metabolism; Science; Science (multidisciplinary); Sequestosome-1 Protein - metabolism; Stress response; Yeast

Autophagy cargo recognition and clearance are essential for intracellular protein quality control. SQSTM1/p62 sequesters intracellular aberrant proteins and mediates cargo delivery for their selective autophagic degradation. The formation of p62 non-membrane-bound liquid compartments is critical for...