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Significance Chaperones are key players in cellular homeostasis that can prevent potentially toxic protein misfolding and aggregation and allow stalled processes to resolve and continue. One of them is a… Click to show full abstract
Significance Chaperones are key players in cellular homeostasis that can prevent potentially toxic protein misfolding and aggregation and allow stalled processes to resolve and continue. One of them is a AAA+ ATPase, p97, that acts as a molecular segregase in many processes in the cell. p97 can be regulated via adaptor proteins and posttranslational modifications. Here we present a structure that captures both regulatory mechanisms at once and explains how remodeling of p97 by the adaptor ASPL enables binding of the p97-modifying methyltransferase METTL21D.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2023
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