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J Am Chem Soc. 2002 Mar 20;124(11):2440-1.

A new strategy for caging proteins regulated by kinases.

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Department of Anatomy and Structural Biology, The Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.


A strategy has been developed for caging proteins that are endogenously regulated by phosphorylation. A key phosphorylatable serine in cofilin, an F-actin cleaving protein, was replaced with a nonphosphorylatable cysteine. The latter conversion ensures that the protein is no longer regulated by endogenous protein kinases. The cysteine residue was subsequently covalently modified with a negatively charged caging moiety, which electrostatically mimics the natural serine phosphate present in the inactive wild-type protein. Photoremoval of the cage generates an active protein, which cannot be switched off by endogenous protein kinases. Caged cofilin, and its irradiated counterpart, display the anticipated F-actin depolymerization and severing activities.

[Indexed for MEDLINE]

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