Mitochondrial chaperones in human health and disease

Bahr, Tyler; Katuri, Joshua; Liang, Ting; Bai, Yidong

doi:10.1016/j.freeradbiomed.2021.11.015

Cited by 22 publications

(24 citation statements)

References 123 publications

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“…Due to their activity in regulating the correct cellular functionality, HSPs are deemed to be powerful therapeutic agents against neurodegenerative diseases [ 178 , 179 , 180 , 181 , 182 ]. In fact, it has been proven that the overexpression of specific HSPs reduces the neurotoxicity of misfolded protein aggregates [ 168 , 171 ].…”

Section: Large-size Proteins and Ad: The Case Of The Heat Shock Prote...mentioning

confidence: 99%

From Small Peptides to Large Proteins against Alzheimer’sDisease

et al. 2022

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Alzheimer’s disease (AD) is the most common neurodegenerative disorder in the elderly. The two cardinal neuropathological hallmarks of AD are the senile plaques, which are extracellular deposits mainly constituted by beta-amyloids, and neurofibrillary tangles formed by abnormally phosphorylated Tau (p-Tau) located in the cytoplasm of neurons. Although the research has made relevant progress in the management of the disease, the treatment is still lacking. Only symptomatic medications exist for the disease, and, in the meantime, laboratories worldwide are investigating disease-modifying treatments for AD. In the present review, results centered on the use of peptides of different sizes involved in AD are presented.

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Section: Large-size Proteins and Ad: The Case Of The Heat Shock Prote...mentioning

confidence: 99%

From Small Peptides to Large Proteins against Alzheimer’sDisease

et al. 2022

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“… 5 Defects in mitochondrial chaperones and chaperonins have been linked to many human diseases. 6 , 7 …”

Section: Introductionmentioning

confidence: 99%

Role of human HSPE1 for OPA1 processing independent of HSPD1

Yeung¹,

Murata²,

Iijima³

et al. 2023

iScience

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“…After maturation, correct folding of mitochondrial proteins is ensured by chaperonins (Horwich and Fenton, 2020). Defects in mitochondrial chaperones and chaperonins have been linked to many human diseases (Bahr et al, 2022; Rodriguez et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

“…In the mitochondrial matrix, two major types of machinery mediate protein folding: the mtHSP70-mtHSP40 system (chaperone) and mtHSP60-mtHSP10 system (chaperonin) (Bahr et al, 2022; Hayer-Hartl et al, 2016; Horwich and Fenton, 2020). The mtHSP70-mtHSP40 system, along with other proteins, facilitates client proteins to be correctly folded during import into the matrix through the translocase of the inner membrane (Bahr et al, 2022; Horwich et al, 1990; Shin et al, 2021; Song and Becker, 2022). The mtHSP60-mtHSP10 system counteracts protein misfolding and unfolding under physiological conditions and in response to different types of stress (Bahr et al, 2022; Song and Becker, 2022).…”

Section: Introductionmentioning

confidence: 99%

“…The mtHSP70-mtHSP40 system, along with other proteins, facilitates client proteins to be correctly folded during import into the matrix through the translocase of the inner membrane (Bahr et al, 2022; Horwich et al, 1990; Shin et al, 2021; Song and Becker, 2022). The mtHSP60-mtHSP10 system counteracts protein misfolding and unfolding under physiological conditions and in response to different types of stress (Bahr et al, 2022; Song and Becker, 2022). The pioneering studies on the founding members of the mtHSP60-mtHSP10 system (the bacterial GroEL-GroES system) revealed that GroEL/mtHSP60 forms a barrel structure with two ring-shaped GroEL/mtHSP60 oligomers (Hayer-Hartl et al, 2016; Horwich and Fenton, 2020; Horwich et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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Role of human HSPE1 for OPA1 processing independent of HSPD1

Sesaki

Iijima

Murata

et al. 2022

Preprint

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The mtHSP60/HSPD1-mtHSP10/HSPE1 system prevents protein misfolding and maintains proteostasis in the mitochondrial matrix. Altered activities of this chaperonin system have been implicated in human diseases, such as cancer and neurodegeneration. However, how defects in HSPD1 and HSPE1 affect mitochondrial structure and dynamics remains elusive. In the current study, we address this fundamental question in a human cell line, HEK293T. We found that the depletion of HSPD1 or HSPE1 results in fragmentation of mitochondria, suggesting a decrease in mitochondrial fusion. Supporting this notion, HSPE1 depletion led to proteolytic inactivation of OPA1, a dynamin-related GTPase that fuses the mitochondrial membrane. This OPA1 inactivation was mediated by a stress-activated metalloprotease, OMA1. In contrast, HSPD1 depletion did not induce OMA1 activation or OPA1 cleavage. These data suggest that HSPE1 controls mitochondrial morphology through a mechanism separate from its chaperonin activity.

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Mitochondrial chaperones in human health and disease

Cited by 22 publications

References 123 publications

From Small Peptides to Large Proteins against Alzheimer’sDisease

From Small Peptides to Large Proteins against Alzheimer’sDisease

Role of human HSPE1 for OPA1 processing independent of HSPD1

Role of human HSPE1 for OPA1 processing independent of HSPD1

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