<i>KIAA0368</i>-deficiency affects disassembly of 26S proteasome under oxidative stress condition

Haratake, Kousuke; Sato, Ayumu; Tsuruta, Fuminori; Chiba, Tomoki

doi:10.1093/jb/mvw006

Cited by 21 publications

(17 citation statements)

References 45 publications

(27 reference statements)

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“…It was suggested that the free CP but not the 26S proteasome mediates degradation of oxidized proteins (Davies 2001;Breusing and Grune 2008). Ecm29-regulated disassembly of the proteasome increases the abundance of the free CP and allows cells to adapt to the oxidative stress (Haratake et al 2016). In addition, by associating with various molecular motors and endosomal components, mammalian ECM29 promotes localization of the proteasome at the ER, the centrosome and likely other cellular locations (Gorbea et al 2004;Gorbea et al 2010).…”

Section: Proteasome-associated Proteinsmentioning

confidence: 99%

Structure, Dynamics and Function of the 26S Proteasome

Mao

2020

Subcellular Biochemistry

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The 26S proteasome is the most complex ATP-dependent protease machinery, of ~2.5 MDa mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated proteins and plays fundamentally indispensable roles in regulating almost all major aspects of cellular activities. To serve as the sole terminal “processor” for myriad ubiquitylation pathways, the proteasome evolved exceptional adaptability in dynamically organizing a large network of proteins, including ubiquitin receptors, shuttle factors, deubiquitinases, AAA-ATPase unfoldases, and ubiquitin ligases, to enable substrate selectivity and processing efficiency and to achieve regulation precision of a vast diversity of substrates. The inner working of the 26S proteasome is among the most sophisticated, enigmatic mechanisms of enzyme machinery in eukaryotic cells. Recent breakthroughs in three-dimensional atomic-level visualization of the 26S proteasome dynamics during polyubiquitylated substrate degradation elucidated an extensively detailed picture of its functional mechanisms, owing to progressive methodological advances associated with cryogenic electron microscopy (cryo-EM). Multiple sites of ubiquitin binding in the proteasome revealed a canonical mode of ubiquitin-dependent substrate engagement. The proteasome conformation in the act of substrate deubiquitylation provided insights into how the deubiquitylating activity of RPN11 is enhanced in the holoenzyme and is coupled to substrate translocation. Intriguingly, three principal modes of coordinated ATP hydrolysis in the heterohexameric AAA-ATPase motor were discovered to regulate intermediate functional steps of the proteasome, including ubiquitin-substrate engagement, deubiquitylation, initiation of substrate translocation and processive substrate degradation. The atomic dissection of the innermost working of the 26S proteasome opens up a new era in our understanding of the ubiquitin-proteasome system and has far-reaching implications in health and disease.

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Section: Proteasome-associated Proteinsmentioning

confidence: 99%

Structure, Dynamics and Function of the 26S Proteasome

Mao

2020

Subcellular Biochemistry

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“…Initially, redox modifications induce a rapid increase in the catalytic activity and proteolytic capacity of pre-existing 20S proteasomes [23,24,25]. In addition, short-term exposure to oxidative stress induces the disassembly of the 26S proteasome complex into 20S and 19S particles [10], a process that is assisted by the yeast proteasome-interacting protein Ecm29 [26] and its mammalian orthologue, KIAA0368 [27]. Ecm29 knockdown results in a significant reduction in 26S proteasome disassembly upon exposure to oxidative stress, which is accompanied with reduced cell survival rates [26].…”

Section: Adaptation To Oxidative Stressmentioning

confidence: 99%

“…Ecm29 knockdown results in a significant reduction in 26S proteasome disassembly upon exposure to oxidative stress, which is accompanied with reduced cell survival rates [26]. On the other hand, mouse KIAA0368 knock-out cells were shown to be more resistant to hydrogen peroxide exposure, in spite of the reduced dissociation of the 26S proteasome into active 20S complexes [27]. Hence, further research is needed, in order to specifically indicate whether the 26S proteasome takes part in eliminating oxidized proteins and whether Ecm29/KIAA0368 is involved in increasing 20S levels by inducing 26S disassembly.…”

Section: Adaptation To Oxidative Stressmentioning

confidence: 99%

The Contribution of the 20S Proteasome to Proteostasis

et al. 2019

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The last decade has seen accumulating evidence of various proteins being degraded by the core 20S proteasome, without its regulatory particle(s). Here, we will describe recent advances in our knowledge of the functional aspects of the 20S proteasome, exploring several different systems and processes. These include neuronal communication, post-translational processing, oxidative stress, intrinsically disordered protein regulation, and extracellular proteasomes. Taken together, these findings suggest that the 20S proteasome, like the well-studied 26S proteasome, is involved in multiple biological processes. Clarifying our understanding of its workings calls for a transformation in our perception of 20S proteasome-mediated degradation—no longer as a passive and marginal path, but rather as an independent, coordinated biological process. Nevertheless, in spite of impressive progress made thus far, the field still lags far behind the front lines of 26S proteasome research. Therefore, we also touch on the gaps in our knowledge of the 20S proteasome that remain to be bridged in the future.

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“…Activation of the adaptive stress response leads to rapid disassembly of the 26S Proteasome by sequestering of the 19S oxidant-inactivated regulatory caps by HSP70 [162, 163]. HSP70 actually acts in conjunction with a partner enzyme, ECM29, first identified as a proteasome scaffolding protein in yeast [164, 165] and later found to have a conserved role in mammalian cells [166, 167]. This leads to an immediate increase in the cytosolic pool of 20S Proteasomes available to degrade oxidized proteins.…”

Section: Adaptive Homeostasis and Ageingmentioning

confidence: 99%

Adaptive homeostasis and the free radical theory of ageing

Pomatto

Davies

2018

Free Radical Biology and Medicine

168

102

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The Free Radical Theory of Ageing, was first proposed by Denham Harman in the mid-1950's, based largely on work conducted by Rebeca Gerschman and Daniel Gilbert. At its core, the Free Radical Theory of Ageing posits that free radical and related oxidants, from the environment and internal metabolism, cause damage to cellular constituents that, over time, result in an accumulation of structural and functional problems. Several variations on the original concept have been advanced over the past six decades, including the suggestion of a central role for mitochondria-derived reactive species, and the proposal of an age-related decline in the effectiveness of protein, lipid, and DNA repair systems. Such innovations have helped the Free Radical Theory of Aging to achieve widespread popularity. Nevertheless, an ever-growing number of apparent 'exceptions' to the Theory have seriously undermined its acceptance. In part, we suggest, this has resulted from a rather simplistic experimental approach of knocking-out, knocking-down, knocking-in, or overexpressing antioxidant-related genes to determine effects on lifespan. In some cases such experiments have yielded results that appear to support the Free Radical Theory of Aging, but there are just as many published papers that appear to contradict the Theory. We suggest that free radicals and related oxidants are but one subset of stressors with which all life forms must cope over their lifespans. Adaptive Homeostasis is the mechanism by which organisms dynamically expand or contract the homeostatic range of stress defense and repair systems, employing a veritable armory of signal transduction pathways (such as the Keap1-Nrf2 system) to generate a complex profile of inducible and enzymatic protection that best fits the particular need. Viewed as a component of Adaptive Homeostasis, the Free Radical Theory of Aging appears both viable and robust.

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KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative stress condition

Cited by 21 publications

References 45 publications

Structure, Dynamics and Function of the 26S Proteasome

Structure, Dynamics and Function of the 26S Proteasome

The Contribution of the 20S Proteasome to Proteostasis

Adaptive homeostasis and the free radical theory of ageing

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