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AN1-type zinc finger protein 1 (ZFAND1) is a cytoplasmic protein containing two AN1-type zinc finger domains and a C-terminal ubiquitin-like domain. It functions in the regulation of cytoplasmic stress granule turnover by mediating the clearance of stress granules (SGs) induced by arsenite and other proteotoxic insults. ZFAND1 interacts with the 26S proteasome and the ATP-dependent chaperone VCP/p97, recruiting them to SGs to facilitate degradation of defective ribosomal products and prevent persistence of aberrant, disease-associated SGs. Loss or mutation of ZFAND1 disrupts normal SG turnover, contributing to proteostasis defects linked to neurodegeneration and cancer. ZFAND1 is not a receptor, enzyme, transporter, or classical drug target, and there are currently no known drugs or clinical biomarkers associated specifically with this protein.
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