Abstract：
:Stress granules (SGs) are cytoplasmic assemblies of mRNPs stalled in translation initiation. They are induced by various stress conditions, including exposure to the environmental toxin and carcinogen arsenic. While perturbed SG turnover is linked to the pathogenesis of neurodegenerative diseases, the molecular mechanisms underlying SG formation and turnover are still poorly understood. Here, we show that ZFAND1 is an evolutionarily conserved regulator of SG clearance. ZFAND1 interacts with two key factors of protein degradation, the 26S proteasome and the ubiquitin-selective segregase p97, and recruits them to arsenite-induced SGs. In the absence of ZFAND1, SGs lack the 26S proteasome and p97, accumulate defective ribosomal products, and persist after arsenite removal, indicating their transformation into aberrant, disease-linked SGs. Accordingly, ZFAND1 depletion is epistatic to the expression of pathogenic mutant p97 with respect to SG clearance, suggesting that ZFAND1 function is relevant to the multisystem degenerative disorder IBMPFD/ALS.
journal_name
Mol Celljournal_title
Molecular cellauthors
Turakhiya A,Meyer SR,Marincola G,Böhm S,Vanselow JT,Schlosser A,Hofmann K,Buchberger Adoi
10.1016/j.molcel.2018.04.021subject
Has Abstractpub_date
2018-06-07 00:00:00pages
906-919.e7issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(18)30317-4journal_volume
70pub_type
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