SIGN IN   Advanced Search

Browse Enzymology
Uncaging Akt

Many signal transduction pathways comprise protein kinase cascades in which the activity of each component is controlled by phosphorylation and dephosphorylation. A new layer of kinase regulation involving nucleotide binding has now been unraveled. Phosphorylation of Akt at two regulatory sites plays a major role in kinase activation. New findings show that adenosine triphosphate (ATP) binding to Akt induces an intramolecular interaction between these phosphorylation sites and other domains in the protein, creating a cage around the phosphate group and restricting the access of phosphatases to these sites. ATP hydrolysis and substrate phosphorylation open the cage, which permits dephosphorylation and inactivation of the kinase. This switchlike mechanism provides important new insights into the biology of protein kinases.

Rate this Resource:
1 = not useful, 5 = very useful

Please be the first to rate this resource.

Subscribe and
View Resource


Resource Type: Bibliography, Diagram, Illustration, Journal article/Issue, Review
Audience Level: Undergraduate upper division 15-16, Graduate, Professional (degree program)

Author and Copyright

Authors and Editors: Sean J. Humphrey of Diabetes and Obesity Program, Garvan Institute of Medical Research, David E. James of Diabetes and Obesity Program, Garvan Institute of Medical Research
Publisher: American Association for the Advancement of Science
Format: application/pdf, image/gif, image/jpeg, text/html
Copyright and other restrictions: Yes
Cost: Yes


» Sign In or register to post comments.

STKE/Science Signaling



Triple A S National Science Foundation Naitonal Science Digital Library Pathway
Funded by the individual BEN Collaborators and grants from the
National Science Foundation [DUE 0085840 / DUE 0226185 / DUE 0532797 / DUE 0734995]

This website is a National Science Digital Library (NSDL) Pathway.
Copyright © 2019. American Association for the Advancement of Science. All Rights Reserved.