Journal
SCIENCE
Volume 309, Issue 5731, Pages 142-145Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1111915
Keywords
-
Categories
Funding
- NCI NIH HHS [T32-CA93247, P01-CA24014] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038663, GM08537, R01 GM38663] Funding Source: Medline
Ask authors/readers for more resources
Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a rheostat for cell signaling to fine-tune transcription at the level of DNA binding.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available