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The Diverging Roles of Calmodulin and PKC in the Regulation of p21 Intracellular Localization
Neus Agell, Montserrat Jaumot, Aina Rodríguez-Vilarrupla, Sonia Brun, Neus Abella Núria Canela, Josep Mª Estanyol and Oriol Bachs
volume 5 | issue 1
1 january 2006Pages: 3 - 6
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Intracellular localization plays an important role in the functional regulation of the cyclindependent kinase inhibitor p21. While nuclear functions have been linked to the tumor suppressor activity of p21, cytoplasmatic functions are oncogenic. We have recently shown that Ser153 phosphorylation of p21 by PKC contributes to its cytoplasmatic accumulation, and that this phosphorylation is inhibited by Ca2+-dependent calmodulin binding to the Cterminal region of p21. Consequently, PKC and calmodulin/Ca2+ play diverging roles in the regulation of p21 intracellular localization. Other kinases such as AKT and MIRK/dyrk1B also phosphorylate p21 near the nuclear localization signal, thus inhibiting its nuclear accumulation. We discuss here the effects of such phosphorylations on p21 functionality, as well as its relevance to cell cycle progression and differentiation.
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.