Phosphorylation puts the pRb tumor suppressor into shape
- Massachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA
Abstract
In this issue of Genes & Development, Burke and colleagues (pp. 1156–1166) describe how the structure of retinoblastoma protein (pRb) is altered by phosphorylation at T373 or S608. These modifications cause specific conformational changes and alter pRb's interaction with E2F via two distinct mechanisms. The structures suggest that the panel of phosphorylation sites represents a versatile set of tools that are used to sculpt pRb in precise, but very different, ways.
Keywords
- Retinoblastoma protein
- cell cycle regulation
- multisite phosphorylation
- cyclin-dependent kinase
- X-ray crystal structure
- small-angle X-ray scattering (SAXS)
Footnotes
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↵1 Corresponding author.
E-mail dyson{at}helix.mgh.harvard.edu.
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Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.195552.112.
- Copyright © 2012 by Cold Spring Harbor Laboratory Press
