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Updated: Jun 20, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
S-acylation of TDP-43: PALMing down aggregation?
1Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Abstract:
S-acylation is well known for regulating protein stability and trafficking. In a recent issue of Molecular Cell, Xu et al.1 reveal a distinct, aggregation-suppressing function of this posttranslational lipid modification: S-acylation of the RNA-binding protein TDP-43 antagonizes poly(ADP-ribose)-driven condensation. Moreover, reduced S-acylation levels are linked to ALS pathogenesis.
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