Another piece of the p27Kip1 puzzle - PubMed (original) (raw)
Review
. 2007 Jan 26;128(2):241-4.
doi: 10.1016/j.cell.2007.01.006.
Affiliations
- PMID: 17254963
- DOI: 10.1016/j.cell.2007.01.006
Free article
Review
Another piece of the p27Kip1 puzzle
Philipp Kaldis. Cell. 2007.
Free article
Abstract
How extracellular signals communicate with the cell cycle is poorly understood. In this issue, two papers address this problem by reporting phosphorylation of the cyclin-dependent kinase inhibitor p27Kip1 on a tyrosine residue by nonreceptor tyrosine kinases, which decreases p27 stability. This new mechanism could explain how cells enter the cell cycle from a quiescent state.
Comment on
- Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases.
Grimmler M, Wang Y, Mund T, Cilensek Z, Keidel EM, Waddell MB, Jäkel H, Kullmann M, Kriwacki RW, Hengst L. Grimmler M, et al. Cell. 2007 Jan 26;128(2):269-80. doi: 10.1016/j.cell.2006.11.047. Cell. 2007. PMID: 17254966 - p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2.
Chu I, Sun J, Arnaout A, Kahn H, Hanna W, Narod S, Sun P, Tan CK, Hengst L, Slingerland J. Chu I, et al. Cell. 2007 Jan 26;128(2):281-94. doi: 10.1016/j.cell.2006.11.049. Cell. 2007. PMID: 17254967 Free PMC article.