How does ATP hydrolysis control actin's associations?

Polymers of actin (F-actin) form an integral part of the structural framework that supports the plasma membrane of our cells while providing a platform for signaling and metabolic proteins. Most subunits in an actin filament hydrolyze a single molecule of ATP to ADP over the F-actin's lifetime. This hydrolysis is the critical timekeeper of F-actin longevity that informs a host of accessory proteins about the state of the filament (1). Here, we discuss the structural changes within each subunit of F-actin that are induced by the nucleotide hydrolysis.

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