Heat shock protein 90 regulates phosphatidylinositol 3-kinase-related protein kinase family proteins together with the RUVBL1/2 and Tel2-containing co-factor complex

2011 ◽  
Vol 103 (1) ◽  
pp. 50-57 ◽  
Author(s):  
Natsuko Izumi ◽  
Akio Yamashita ◽  
Hisashi Hirano ◽  
Shigeo Ohno
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Related Protein ◽  
Phosphatidylinositol 3 Kinase ◽  
Protein Kinase Family ◽  
Kinase Family ◽  
Phosphatidylinositol 3

scholarly journals Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

2012 ◽  
Vol 92 (4) ◽  
pp. 1577-1617 ◽  
Author(s):  
Kenneth B. Gagnon ◽  
Eric Delpire
Keyword(s):  
Protein Kinase ◽  
Multiple Organ ◽  
Genetically Engineered ◽  
Related Protein ◽  
Molecular Physiology ◽  
Cancer Proliferation ◽  
Protein Kinase Family ◽  
Kinase Family ◽  
Organ Systems ◽  
And Migration

SPAK (Ste20-related proline alanine rich kinase) and OSR1 (oxidative stress responsive kinase) are members of the germinal center kinase VI subfamily of the mammalian Ste20 (Sterile20)-related protein kinase family. Although there are 30 enzymes in this protein kinase family, their conservation across the fungi, plant, and animal kingdom confirms their evolutionary importance. Already, a large volume of work has accumulated on the tissue distribution, binding partners, signaling cascades, and physiological roles of mammalian SPAK and OSR1 in multiple organ systems. After reviewing this basic information, we will examine newer studies that demonstrate the pathophysiological consequences to SPAK and/or OSR1 disruption, discuss the development and analysis of genetically engineered mouse models, and address the possible role these serine/threonine kinases might have in cancer proliferation and migration.

SNF1-related protein kinase (SnRK1) phosphorylates class I heat shock protein

2004 ◽  
Vol 42 (2) ◽  
pp. 111-116 ◽  
Author(s):  
Stephen P Slocombe ◽  
Frédéric Beaudoin ◽  
Paul G Donaghy ◽  
D.Grahame Hardie ◽  
J.Richard Dickinson ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Class I ◽  
Related Protein

scholarly journals Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability

2003 ◽  
Vol 370 (3) ◽  
pp. 849-857 ◽  
Author(s):  
Jérôme BOUDEAU ◽  
Maria DEAK ◽  
Margaret A. LAWLOR ◽  
Nick A. MORRICE ◽  
Dario R. ALESSI
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Kinase Domain ◽  
Cancer Syndrome ◽  
Hsp90 Inhibitors ◽  
Detailed Mechanism ◽  
Anti Cancer ◽  
Hsp90 Chaperone

LKB1 is a widely expressed serine/threonine protein kinase that is mutated in the inherited Peutz—Jeghers cancer syndrome. Recent findings indicate that LKB1 functions as a tumour suppressor, but little is known regarding the detailed mechanism by which LKB1 regulates cell growth. In this study we have purified LKB1 from cells and establish that it is associated with the heat-shock protein 90 (Hsp90) chaperone and the Cdc37 kinase-specific targetting subunit for Hsp90. We demonstrate that Cdc37 and Hsp90 bind specifically to the kinase domain of LKB1. We also perform experiments using Hsp90 inhibitors, which indicate that the association of Hsp90 and Cdc37 with LKB1 regulates LKB1 stability and prevents its degradation by the proteasome. Hsp90 inhibitors are being considered as potential anti-cancer agents. However, our observations indicate that prolonged usage of these drugs could possibly lead to tumour development by decreasing cellular levels of LKB1.

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