Inhibition of the Ubiquitin-Proteasome Pathway Induces Differential Heat-Shock Protein Response in Cardiomyocytes and Renders Early Cardiac Protection

2002 ◽  
Vol 291 (3) ◽  
pp. 542-549 ◽  
Author(s):  
Karl Stangl ◽  
Christoph Günther ◽  
Thomas Frank ◽  
Mario Lorenz ◽  
Silke Meiners ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cardiac Protection ◽  
Differential Heat ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
Protein Response

scholarly journals Heat Shock Protein 70 Regulates Degradation of the Mumps Virus Phosphoprotein via the Ubiquitin-Proteasome Pathway

2014 ◽  
Vol 89 (6) ◽  
pp. 3188-3199 ◽  
Author(s):  
Hiroshi Katoh ◽  
Toru Kubota ◽  
Shunsuke Kita ◽  
Yuichiro Nakatsu ◽  
Natsuko Aoki ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Cytoplasmic Inclusion ◽  
Mumps Virus ◽  
Viral Rna ◽  
Ubiquitin Proteasome Pathway ◽  
P Protein ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

ABSTRACTMumps virus (MuV) infection induces formation of cytoplasmic inclusion bodies (IBs). Growing evidence indicates that IBs are the sites where RNA viruses synthesize their viral RNA. However, in the case of MuV infection, little is known about the viral and cellular compositions and biological functions of the IBs. In this study, pulldown purification and N-terminal amino acid sequencing revealed that stress-inducible heat shock protein 70 (Hsp72) was a binding partner of MuV phosphoprotein (P protein), which was an essential component of the IB formation. Immunofluorescence and immunoblotting analyses revealed that Hsp72 was colocalized with the P protein in the IBs, and its expression was increased during MuV infection. Knockdown of Hsp72 using small interfering RNAs (siRNAs) had little, if any, effect on viral propagation in cultured cells. Knockdown of Hsp72 caused accumulation of ubiquitinated P protein and delayed P protein degradation. These results show that Hsp72 is recruited to IBs and regulates the degradation of MuV P protein through the ubiquitin-proteasome pathway.IMPORTANCEFormation of cytoplasmic inclusion bodies (IBs) is a common characteristic feature in mononegavirus infections. IBs are considered to be the sites of viral RNA replication and transcription. However, there have been few studies focused on host factors recruited to the IBs and their biological functions. Here, we identified stress-inducible heat shock protein 70 (Hsp72) as the first cellular partner of mumps virus (MuV) phosphoprotein (P protein), which is an essential component of the IBs and is involved in viral RNA replication/transcription. We found that the Hsp72 mobilized to the IBs promoted degradation of the MuV P protein through the ubiquitin-proteasome pathway. Our data provide new insight into the role played by IBs in mononegavirus infection.

scholarly journals The Degradation of Apolipoprotein B100 Is Mediated by the Ubiquitin-proteasome Pathway and Involves Heat Shock Protein 70

1997 ◽  
Vol 272 (33) ◽  
pp. 20427-20434 ◽  
Author(s):  
Edward A. Fisher ◽  
Mingyue Zhou ◽  
Deborah M. Mitchell ◽  
Xujun Wu ◽  
Satoshi Omura ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Ubiquitin Proteasome Pathway ◽  
Apolipoprotein B100 ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

scholarly journals The ubiquitin/proteasome pathway from Lemna minor subjected to heat shock

2008 ◽  
Vol 52 (4) ◽  
pp. 695-702 ◽  
Author(s):  
A. S. Caeiro ◽  
P. C. Ramos ◽  
A. R. Teixeira ◽  
R. B. Ferreira
Keyword(s):  
Heat Shock ◽  
Lemna Minor ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

Pim-1 Kinase Stability Is Regulated by Heat Shock Proteins and the Ubiquitin-Proteasome Pathway

2005 ◽  
Vol 3 (3) ◽  
pp. 170-181 ◽  
Author(s):  
Kate Petersen Shay ◽  
Zeping Wang ◽  
Pei-xiang Xing ◽  
Ian F.C. McKenzie ◽  
Nancy S. Magnuson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ubiquitin Proteasome Pathway ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
Shock Proteins

scholarly journals Heat Shock Response and Protein Degradation: Regulation of HSF2 by the Ubiquitin-Proteasome Pathway

1998 ◽  
Vol 18 (9) ◽  
pp. 5091-5098 ◽  
Author(s):  
Anu Mathew ◽  
Sameer K. Mathur ◽  
Richard I. Morimoto
Keyword(s):  
Heat Shock ◽  
Mammalian Cells ◽  
Proteasome Inhibitors ◽  
Heat Shock Gene ◽  
Heat Shock Factors ◽  
Heat Shock Genes ◽  
Ubiquitin Proteasome Pathway ◽  
Stress Signal ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

ABSTRACT Mammalian cells coexpress a family of heat shock factors (HSFs) whose activities are regulated by diverse stress conditions to coordinate the inducible expression of heat shock genes. Distinct from HSF1, which is expressed ubiquitously and activated by heat shock and other stresses that result in the appearance of nonnative proteins, the stress signal for HSF2 has not been identified. HSF2 activity has been associated with development and differentiation, and the activation properties of HSF2 have been characterized in hemin-treated human K562 erythroleukemia cells. Here, we demonstrate that a stress signal for HSF2 activation occurs when the ubiquitin-proteasome pathway is inhibited. HSF2 DNA-binding activity is induced upon exposure of mammalian cells to the proteasome inhibitors hemin, MG132, and lactacystin, and in the mouse ts85 cell line, which carries a temperature sensitivity mutation in the ubiquitin-activating enzyme (E1) upon shift to the nonpermissive temperature. HSF2 is labile, and its activation requires both continued protein synthesis and reduced degradation. The downstream effect of HSF2 activation by proteasome inhibitors is the induction of the same set of heat shock genes that are induced during heat shock by HSF1, thus revealing that HSF2 affords the cell with a novel heat shock gene-regulatory mechanism to respond to changes in the protein-degradative machinery.

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