2021
DOI: 10.1016/j.jbc.2021.101134
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Proteomic analysis demonstrates the role of the quality control protease LONP1 in mitochondrial protein aggregation

Abstract: This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, a… Show more

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Cited by 17 publications
(14 citation statements)
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References 66 publications
(114 reference statements)
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“…The similar levels of PRKN activation in young and açaí-treated aged oocytes suggest that the mitochondrial quality was improved by açaí such that mitophagy was not triggered. The improved oocyte quality was likely not due to mitochondrial protein quality control, as the activation of the mitochondrial UPR—as determined by LonP1 and HSP60 protein levels—was blunted in aged oocytes, as previously observed [ 44 ], and this was not affected by antioxidants.…”
Section: Discussionsupporting
confidence: 70%
“…The similar levels of PRKN activation in young and açaí-treated aged oocytes suggest that the mitochondrial quality was improved by açaí such that mitophagy was not triggered. The improved oocyte quality was likely not due to mitochondrial protein quality control, as the activation of the mitochondrial UPR—as determined by LonP1 and HSP60 protein levels—was blunted in aged oocytes, as previously observed [ 44 ], and this was not affected by antioxidants.…”
Section: Discussionsupporting
confidence: 70%
“…However, siRNA-induced LonP1 disruption did not induce any of the above stress response pathways in WM266-4 metastatic melanoma cells, advocating in favor of the presence of additional compensatory mechanisms, owing to specific cellular demands. Similarly, a stable genetic LONP1 knockdown (gKD) in HeLa cells, with a significant reduction in cellular protein levels, did not cause severe alterations in mitochondrial structure and function or strong defects in mitochondrial protein degradation efficiency, at least under normal conditions [99].…”
Section: Discussionmentioning
confidence: 99%
“…LONP1 reduces the effects of stress via the degradation of oxidatively damaged and misfolded proteins [ 20 , 44 ]. SIRT3 post-translationally regulates LONP1 via deacetylation.…”
Section: Discussionmentioning
confidence: 99%
“…FB 2 did not alter LONP1 expression despite the downregulation of SIRT3 ( Figure 4 C) and upregulation of ROS ( Figure 2 A). LONP1 (an ATP-dependent protease) contains a highly conserved ATPase domain with an AAA + module and a proteolytic domain with an N-terminal domain [ 20 , 44 ]. FB 2 depleted cellular ATP levels and consequently may have inhibited LONP1 catalytic activity and the degradation of oxidised proteins ( Figure 3 A).…”
Section: Discussionmentioning
confidence: 99%