akt1 sequentially phosphorylates p27kip1 within a conserved but non-canonical region顺序akt1磷酸化p27kip1守恒的但非规范地区.pdfVIP
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akt1 sequentially phosphorylates p27kip1 within a conserved but non-canonical region顺序akt1磷酸化p27kip1守恒的但非规范地区
Cell Division BioMed Central
Research Open Access
Akt1 sequentially phosphorylates p27kip1 within a conserved but
non-canonical region
2 1,2
Lucas P Nacusi and Robert J Sheaff *
Address: 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Cancer Center, University of Minnesota,
Minneapolis MN 55455, USA 2Department of Chemistry and Biochemistry, The University of Tulsa, Tulsa, Oklahoma 74104, USA
Email: Lucas P Nacusi - nacu0001@; Robert J Sheaff* - sheaf004@
* Corresponding author
Published: 16 June 2006 Received: 30 March 2006
Accepted: 16 June 2006
Cell Division 2006, 1:11 doi:10.1186/1747-1028-1-11
This article is available from: /content/1/1/11
© 2006 Nacusi and Sheaff; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0),
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
Background: p27kip1 (p27) is a multifunctional protein implicated in regulation of cell cycling, signal transduction, and
adhesion. Its activity is controlled in part by Phosphatylinositol-3-Kinase (PI3K)/Akt1 signaling, and disruption of this
regulatory connection has been identified in human breast cancers. The serine/threonine protein kinase Akt1 directly
phosphorylates p27, so identifying the modified residue(s) is essential for understanding how it regulates p27 func
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