Journal
GENES & DEVELOPMENT
Volume 26, Issue 11, Pages 1128-1130Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.195552.112
Keywords
Retinoblastoma protein; cell cycle regulation; multisite phosphorylation; cyclin-dependent kinase; X-ray crystal structure; small-angle X-ray scattering (SAXS)
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Funding
- NIH [CA64402]
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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.
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