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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Yang Y,Willis TL,Button RW,Strang CJ,Fu Y,Wen X,Grayson PRC,Evans T,Sipthorpe RJ,Roberts SL,Hu B,Zhang J,Lu B,Luo S

doi

10.1038/s41467-019-11671-2

subject

Has Abstract

pub_date

2019-08-21 00:00:00

pages

3759

issue

1

issn

2041-1723

pii

10.1038/s41467-019-11671-2

journal_volume

10

pub_type

杂志文章

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