Regulation of Cellular Protein Phosphatase-1 (PP1) by Phosphorylation of the CPI-17 Family, C-kinase-activated PP1 Inhibitors

被引：117

作者：

Eto, Masumi ^{[1
,2
]}

机构：

[1] Thomas Jefferson Univ, Dept Mol Physiol & Biophys, Philadelphia, PA 19107 USA

[2] Thomas Jefferson Univ, Kimmel Canc Ctr, Philadelphia, PA 19107 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2009年 / 284卷 / 51期

基金：

美国国家卫生研究院;

关键词：

LIGHT-CHAIN PHOSPHATASE; ARTERIAL SMOOTH-MUSCLE; INTEGRIN-LINKED KINASE; MYOSIN PHOSPHATASE; CA2+ SENSITIZATION; PHOSPHOPROTEIN INHIBITOR; MEDIATED ACTIVATION; INDUCED CONTRACTION; STRUCTURAL BASIS; UP-REGULATION;

D O I：

10.1074/jbc.R109.059972

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The regulatory circuit controlling cellular protein phosphatase-1 (PP1), an abundant group of Ser/Thr phosphatases, involves phosphorylation of PP1-specific inhibitor proteins. Malfunctions of these inhibitor proteins have been linked to a variety of diseases, including cardiovascular disease and cancer. Upon phosphorylation at Thr(38), the 17-kDa PP1 inhibitor protein, CPI-17, selectively inhibits a specific form of PP1, myosin light chain phosphatase, which transduces multiple kinase signals into the phosphorylation of myosin II and other proteins. Here, the mechanisms underlying PP1 inhibition and the kinase/PP1 cross-talk mediated by CPI-17 and its related proteins, PHI, KEPI, and GBPI, are discussed.

引用

页码：35273 / 35277

页数：5

共 60 条

[1] Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56δ subunit
Ahn, Jung-Hyuck
McAvoy, Thomas
Rakhilin, Sergey V.
Nishi, Akinori
Greengard, Paul
Nairn, Angus C.
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (08) : 2979 - 2984
[2] Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling in neurons
Bibb, JA
Snyder, GL
Nishi, A
Yan, Z
Meijer, L
Fienberg, AA
Tsai, LH
Kwon, YT
Girault, JA
Czernik, AJ
Huganir, RL
Hemmings, HC
Nairn, AC
Greengard, P
[J]. NATURE, 1999, 402 (6762) : 669 - 671
[3] Actions downstream of cyclic GMP/protein kinase G can reverse protein kinase C-mediated phosphorylation of CPI-17 and Ca2+ sensitization in smooth muscle
Bonnevier, J
Arner, A
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (28) : 28998 - 29003
[4] Functional diversity of protein phosphatase-1, a cellular economizer and reset button
Ceulemans, H
Bollen, M
[J]. PHYSIOLOGICAL REVIEWS, 2004, 84 (01) : 1 - 39
[5] Increased basal phosphorylation of detrusor smooth muscle myosin in alloxan-induced diabetic rabbit is mediated by upregulation of Rho-kinase β and CPI-17
Chang, SH
Hypolite, JA
DiSanto, ME
Changolkar, A
Wein, AJ
Chacko, S
[J]. AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY, 2006, 290 (03) : F650 - F656
[6] Cohen PTW, 2002, J CELL SCI, V115, P241
[7] Regulation of pulmonary arterial myosin phosphatase activity in neonatal circulatory transition and in hypoxic pulmonary hypertension: A role for CPI-17
Dakshinamurti, S
Mellow, L
Stephens, NL
[J]. PEDIATRIC PULMONOLOGY, 2005, 40 (05) : 398 - 407
[8] Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase
Deng, JT
Sutherland, C
Brautigan, DL
Eto, M
Walsh, MP
[J]. BIOCHEMICAL JOURNAL, 2002, 367 : 517 - 524
[9] Ca2+ dependent rapid Ca2+ sensitization of contraction in arterial smooth muscle
Dimopoulos, George J.
Semba, Shingo
Kitazawa, Kazuyo
Eto, Masumi
Kitazawa, Toshio
[J]. CIRCULATION RESEARCH, 2007, 100 (01) : 121 - 129
[10] Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17
Dubois, T
Howell, S
Zemlickova, E
Learmonth, M
Cronshaw, A
Aitken, A
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 302 (02) : 186 - 192

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