Unravelling the activation mechanisms of protein kinase B/Akt

被引：337

作者：

Scheid, MP ^{[1
]}

Woodgett, JR ^{[1
]}

机构：

[1] Ontario Canc Inst, Toronto, ON M5G 2M9, Canada

来源：

FEBS LETTERS | 2003年 / 546卷 / 01期

关键词：

protein kinase; signal transduction; protein kinase B; Akt; 3-phosphoinositide-dependent kinase-1; phosphatidylinositol; 3-kinase;

D O I：

10.1016/S0014-5793(03)00562-3

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：

Over the past decade, protein kinase B (PKB, also termed Akt) has emerged as an important signaling mediator between extracellular cues and modulation of gene expression, metabolism, and cell survival. The enzyme is tightly controlled and consequences of its deregulation include loss of growth control and oncogenesis. Recent work has better characterized the mechanism of PKB activation, including upstream regulators and secondary binding partners. This minireview refreshes some old concepts with new twists and highlights current outstanding questions. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：108 / 112

页数：5

共 40 条

[1] Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha
Alessi, DR
James, SR
Downes, CP
Holmes, AB
Gaffney, PRJ
Reese, CB
Cohen, P
[J]. CURRENT BIOLOGY, 1997, 7 (04) : 261 - 269
[2] Mechanism of activation of protein kinase B by insulin and IGF-1
Alessi, DR
Andjelkovic, M
Caudwell, B
Cron, P
Morrice, N
Cohen, P
Hemmings, BA
[J]. EMBO JOURNAL, 1996, 15 (23) : 6541 - 6551
[3] Andjelkovic M, 1999, MOL CELL BIOL, V19, P5061
[4] A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Cζ (PKCζ) and PKC-related kinase 2 by PDK1
Balendran, A
Biondi, RM
Cheung, PCF
Casamayor, A
Deak, M
Alessi, DR
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (27) : 20806 - 20813
[5] PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
Balendran, A
Casamayor, A
Deak, M
Paterson, A
Gaffney, P
Currie, R
Downes, CP
Alessi, DR
[J]. CURRENT BIOLOGY, 1999, 9 (08) : 393 - 404
[6] Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis
Batkin, M
Schvartz, I
Shaltiel, S
[J]. BIOCHEMISTRY, 2000, 39 (18) : 5366 - 5373
[7] The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
Biondi, RM
Kieloch, A
Currie, RA
Deak, M
Alessi, DR
[J]. EMBO JOURNAL, 2001, 20 (16) : 4380 - 4390
[8] High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
Biondi, RM
Komander, D
Thomas, CC
Lizcano, JM
Deak, M
Alessi, DR
van Aalten, DMF
[J]. EMBO JOURNAL, 2002, 21 (16) : 4219 - 4228
[9] Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
Biondi, RM
Nebreda, AR
[J]. BIOCHEMICAL JOURNAL, 2003, 372 : 1 - 13
[10] Regulation of Akt/PKB activation by tyrosine phosphorylation
Chen, RY
Kim, O
Yang, JB
Sato, K
Eisenmann, KM
McCarthy, J
Chen, HG
Qiu, Y
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (34) : 31858 - 31862

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