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

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...

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Published inNature 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
LanguageEnglish
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
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Abstract 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 its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX. The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.
AbstractList The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.
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 its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX. The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.
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 its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX.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 its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX.
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 its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX.
ArticleNumber 3759
Author Luo, Shouqing
Hu, Bing
Button, Robert W.
Grayson, Portia R. C.
Evans, Tracey
Strang, Conor J.
Willis, Thea L.
Zhang, Jianke
Wen, Xue
Sipthorpe, Rebecca J.
Lu, Boxun
Roberts, Sheridan L.
Yang, Yi
Fu, Yuhua
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31434890$$D View this record in MEDLINE/PubMed
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Snippet Autophagy cargo recognition and clearance are essential for intracellular protein quality control. SQSTM1/p62 sequesters intracellular aberrant proteins and...
The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone...
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StartPage 3759
SubjectTerms 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
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Title Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
URI https://link.springer.com/article/10.1038/s41467-019-11671-2
https://www.ncbi.nlm.nih.gov/pubmed/31434890
https://www.proquest.com/docview/2277417856
https://www.proquest.com/docview/2320872484
https://pubmed.ncbi.nlm.nih.gov/PMC6704147
https://doaj.org/article/63468e0902e8452ea56c0ff4e2ec70b3
Volume 10
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