scholarly journals Serine 389 phosphorylation of 3-phosphoinositide-dependent kinase 1 by UNC-51-like kinase 1 affects its ability to regulate Akt and p70 S6kinase

BMB Reports ◽  
2020 ◽  
Vol 53 (7) ◽  
pp. 373-378
Author(s):  
Kidae Kim ◽  
Sung Goo Park ◽  
Byoung Chul Park ◽  
Jeong-Hoon Kim ◽  
Sunhong Kim
Keyword(s):  
Phosphoinositide Dependent Kinase

Structure-Based Design of Potent and Selective 3-Phosphoinositide-Dependent Kinase-1 (PDK1) Inhibitors

2011 ◽  
Vol 54 (6) ◽  
pp. 1871-1895 ◽  
Author(s):  
Jesús R. Medina ◽  
Christopher J. Becker ◽  
Charles W. Blackledge ◽  
Celine Duquenne ◽  
Yanhong Feng ◽  
...  
Keyword(s):  
Phosphoinositide Dependent Kinase

scholarly journals Requirement for 3-Phosphoinositide-dependent Kinase-1 (PDK-1) in Insulin-induced Glucose Uptake in Immortalized Brown Adipocytes

2003 ◽  
Vol 278 (40) ◽  
pp. 38870-38874 ◽  
Author(s):  
Hiroshi Sakaue ◽  
Akihiko Nishizawa ◽  
Wataru Ogawa ◽  
Kiyoshi Teshigawara ◽  
Toshiyuki Mori ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Brown Adipocytes ◽  
Phosphoinositide Dependent Kinase

Phosphoinositide-dependent kinase-1 inhibits TRAF6 ubiquitination by interrupting the formation of TAK1–TAB2 complex in TLR4 signaling

2015 ◽  
Vol 27 (12) ◽  
pp. 2524-2533 ◽  
Author(s):  
Gyuyoung Moon ◽  
Juhong Kim ◽  
Yoon Min ◽  
Sae Mi Wi ◽  
Jae-Hyuck Shim ◽  
...  
Keyword(s):  
Tlr4 Signaling ◽  
Phosphoinositide Dependent Kinase

For a PDK1 inhibitor, the substrate matters

2010 ◽  
Vol 433 (2) ◽  
pp. e1-e2 ◽  
Author(s):  
Zachary A. Knight
Keyword(s):  
Cell Growth ◽  
Protein Kinases ◽  
Cell Signalling ◽  
Central Component ◽  
Specific Inhibition ◽  
Biochemical Journal ◽  
Regulate Cell Growth ◽  
Kinetics Of ◽  
Kinetics Of Inhibition ◽  
Phosphoinositide Dependent Kinase

More than 20 protein kinases are directly activated by 3-phosphoinositide-dependent kinase 1 (PDK1), which is a central component of the pathways that regulate cell growth, proliferation and survival. Despite the importance of PDK1 in cell signalling, highly selective PDK1 inhibitors have not been described. In this issue of the Biochemical Journal, Dario Alessi's group and their collaborators at GlaxoSmithKline report GSK2334470, a potent and selective PDK1 inhibitor. They show that this compound blocks the phosphorylation of known PDK1 substrates, but surprisingly find that the potency and kinetics of inhibition vary for different PDK1 targets. This substrate-specific inhibition has implications for the development of PDK1 inhibitors as drugs.

Sign in / Sign up

Export Citation Format

Share Document