HomeAbout

SIGN IN   Advanced Search










 
Browse Illustration
Reversible Phosphorylation of Histidine Residues in Proteins from Vertebrates

Signaling by kinases and phosphatases that act on serine, threonine, and tyrosine residues of proteins is among the most extensively studied regulatory mechanisms in mammalian cells, and research focused in this area is ongoing. We are just beginning to appreciate that such signaling mechanisms are extended and enriched by the reversible phosphorylation of histidine residues. The most exciting developments in this field to date come from studies on the β subunit of heterotrimeric guanosine triphosphate–binding proteins (G proteins), the enzyme adenosine 5′-triphosphate-citrate lyase, and now the Ca2+-activated K+ channel KCa3.1, all of which are targeted by nucleoside diphosphate kinase (which phosphorylates histidines) and protein histidine phosphatase (which dephosphorylates phosphorylated histidines).

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

Please be the first to rate this resource.


Subscribe and
View Resource

Classifications


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: Susanne Klumpp of Westfalische Wilhelms-Universitat, Munster, Josef Krieglstein of Westfalische Wilhelms-Universitat, Munster
Publisher: American Association for the Advancement of Science
Format: application/pdf, image/gif, image/jpeg, text/html
Copyright and other restrictions: Yes
Cost: Yes

Comments


» Sign In or register to post comments.


Collection:
STKE/Science Signaling


     
   

SITE MAP | CONTACT | POLICIES

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.