The diverging roles of calmodulin and PKC in the regulation of p21 intracellular localization

被引：16

作者：

Agell, N ^{[1
]}

Jaumot, M ^{[1
]}

Rodríguez-Vilarrupla, A ^{[1
]}

Brun, S ^{[1
]}

Abella, N ^{[1
]}

Canela, N ^{[1
]}

Estanyol, JM ^{[1
]}

机构：

[1] Univ Barcelona, Dept Biol Cellular & Anat Patol, Fac Med, Inst Invest Biomed August Pi & Sunyer IDIBAPS, E-08036 Barcelona, Spain

来源：

CELL CYCLE | 2006年 / 5卷 / 01期

关键词：

p21; calmodulin; PKC; AKT; MIRK/dyrk1B; phosphorylation; intracellular localization; Cdk; CKI;

D O I：

10.4161/cc.5.1.2270

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 [细胞生物学]; 090102 [作物遗传育种];

摘要：

Intracellular localization plays an important role in the functional regulation of the cyclin-dependent 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 C-terminal 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.

引用

页码：3 / 6

页数：4

共 22 条

[1]

Apoptosis inhibitory activity of cytoplasmic p21Cip1/WAF1 in monocytic differentiation [J].