Protein quality control gets muscle into shape

Kim, Johnny; Löwe, Thomas; Hoppe, Thorsten

doi:10.1016/j.tcb.2008.03.007

Cited by 58 publications

(68 citation statements)

References 89 publications

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“…ASK1 is activated in response to various extracellular and intracellular stimuli, such as lipopolysaccharide, ROS, endoplasmic reticulum (ER) stress, and signaling through Fas and TNFa (Matsukawa et al 2004). ASK1 is well known as a proapoptotic, stress-activated signaling molecule, and it is under tight regulation at multiple levels, one of which is negatively regulated by PRDX1 (Kim et al 2008). In this study, we demonstrated that ASK1 played an essential role in MG132-mediated thyroid cancer cell death, as ASK1 knockdown by siRNA markedly suppressed the cytotoxical effects of MG132.…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that PRDX1 negatively regulates ASK1 activity (Kim et al 2008), we hypothesized that induction of PRDX1 may affect MG132-induced apoptosis via its influence on the activation of ASK1.…”

Section: Suppression Of Mg132-mediated Ask1 Activation By Prdx1mentioning

confidence: 99%

“…ASK1 is activated in response to various stresses and plays a critical role in the regulation of signaling in response to oxidative stress, which is a major contributor to proteotoxic damage and cell death , Goldman et al 2004. Recently, PRDX1 has been reported to function as a negative regulator of ASK1 activity (Kim et al 2008), further suggesting a role for PRDX1 in protecting cancer cells from harmful stimuli.…”

Section: Introductionmentioning

confidence: 99%

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Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Du¹,

Yan²,

Zhang³

et al. 2010

Endocrine-Related Cancer

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Proteasome inhibitors represent a novel class of antitumor agents with pre-clinical and clinical evidence of activity against hematologic malignancies and solid tumors. However, emerging evidence indicates that antiapoptotic factors may also accumulate as a consequence of exposure to these drugs, thus it seems plausible that the activation of survival signaling cascades might compromise their antitumoral effects. Peroxiredoxins (PRDXs) are a family of thiol-containing peroxidases identified primarily by their ability to remove cellular hydroperoxides. The function of PRDX1 in particular has been implicated in regulating cell proliferation, differentiation, and apoptosis. Another important finding is that aberrant upregulation of PRDX1 has been discovered in various cancers. Apoptosis signal-regulating kinase 1 (ASK1) is a mitogen-activated protein kinase (MAPK) kinase kinase that is regulated under conditions of cellular stress. ASK1 phosphorylates c-Jun N-terminal kinase and p38 MAPK, and elicits an apoptotic response. ASK1 activity is regulated at multiple levels, one of which is through interaction with PRDX1. In this study, for the first time we report that upregulation of PRDX1 expression was found in thyroid cancer cells treated with proteasome inhibitors, and PRDX1 knockdown resulted in accelerated proteasome inhibitor-induced cell death. In addition, we demonstrated that ASK1 activity was implicated in the PRDX1-dependent response of thyroid cancer cells to proteasome inhibitormediated cell death.

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Section: Discussionmentioning

confidence: 99%

Section: Suppression Of Mg132-mediated Ask1 Activation By Prdx1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Du¹,

Yan²,

Zhang³

et al. 2010

Endocrine-Related Cancer

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“…This complex also plays a critical anabolic role in myofibril assembly in Caenorhabditis elegans (52). It is noteworthy that levels of p97 were markedly increased in the FIGURE 9.…”

Section: The Content Of Ubiquitylated Proteins Increases In Aged Muscmentioning

confidence: 94%

“…6C). In C. elegans, the chaperone unc45B catalyzes myosin filament formation and is then degraded in a process involving p97 and the ubiquitin ligases CHIP and Ufd2 (52). The levels of Unc45 were lower in the aged muscles, suggesting a decline in assembly of new myofibrils.…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

Altun

Besche

Overkleeft

et al. 2010

Journal of Biological Chemistry

197

155

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Among the hallmarks of aged organisms are an accumulation of misfolded proteins and a reduction in skeletal muscle mass ("sarcopenia"). We have examined the effects of aging and dietary restriction (which retards many age-related changes) on components of the ubiquitin proteasome system (UPS) in muscle. The hindlimb muscles of aged (30 months old) rats showed a marked loss of muscle mass and contained 2-3-fold higher levels of 26S proteasomes than those of adult (4 months old) controls. 26S proteasomes purified from muscles of aged and adult rats showed a similar capacity to degrade peptides, proteins, and an ubiquitylated substrate, but differed in levels of proteasome-associated proteins (e.g. the ubiquitin ligase E6AP and deubiquitylating enzyme USP14). Also, the activities of many other deubiquitylating enzymes were greatly enhanced in the aged muscles. Nevertheless, their content of polyubiquitylated proteins was higher than in adult animals. The aged muscles contained higher levels of the ubiquitin ligase CHIP, involved in eliminating misfolded proteins, and MuRF1, which ubiquitylates myofibrillar proteins. These muscles differed from ones rapidly atrophying due to disease, fasting, or disuse in that Atrogin-1/MAFbx expression was low and not inducible by glucocorticoids. Thus, the muscles of aged rats showed many adaptations indicating enhanced proteolysis by the UPS, which may enhance their capacity to eliminate misfolded proteins and seems to contribute to the sarcopenia. Accordingly, dietary restriction decreased or prevented the aging-associated increases in proteasomes and other UPS components and reduced muscle wasting.

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Drosophila and Mouse Models of Hereditary Myopathy Caused by Mutations in VCP/p97

Badders

Taylor

2011

Muscle Aging, Inclusion‐Body Myositis and Myopathies

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Protein quality control gets muscle into shape

Cited by 58 publications

References 89 publications

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

Drosophila and Mouse Models of Hereditary Myopathy Caused by Mutations in VCP/p97

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