HSP60 possesses a GTPase activity and mediates protein folding with HSP10

Okamoto, Tomoya; Yamamoto, Hiroshi; Kudo, Ikuru; Matsumoto, Kazuya; Odaka, Masafumi; Grave, Ewa

doi:10.1038/s41598-017-17167-7

Cited by 32 publications

(23 citation statements)

References 26 publications

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“…Mortalin also interacts with HSP60 (heat shock 60 kDa protein), one of the most important components of the protein folding machinery in the matrix, helping with the proper folding of newly imported proteins (Deocaris et al, 2006 ). The HSP60 and HSP10 (heat shock 10 kDa protein) machineries form two stacked rings in the mitochondrial matrix that allow accommodation of the unfolded polypeptide following the hydrolysis of ATP, assisting henceforth its proper folding (Walter, 2002 ; Okamoto et al, 2017 ). TRAP1 (tumor necrosis factor receptor-associated protein 1), another molecular chaperone present in the matrix, was first identified as a member of the HSP90 (heat shock 90 kDa protein) family because of its high degree of sequence and structural similarity.…”

Section: Mitochondrial Protein Quality Control: the Guarantee Of Mitomentioning

confidence: 99%

Mitochondrial Quality Control in Neurodegenerative Diseases: Focus on Parkinson's Disease and Huntington's Disease

2018

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In recent years, several important advances have been made in our understanding of the pathways that lead to cell dysfunction and death in Parkinson's disease (PD) and Huntington's disease (HD). Despite distinct clinical and pathological features, these two neurodegenerative diseases share critical processes, such as the presence of misfolded and/or aggregated proteins, oxidative stress, and mitochondrial anomalies. Even though the mitochondria are commonly regarded as the “powerhouses” of the cell, they are involved in a multitude of cellular events such as heme metabolism, calcium homeostasis, and apoptosis. Disruption of mitochondrial homeostasis and subsequent mitochondrial dysfunction play a key role in the pathophysiology of neurodegenerative diseases, further highlighting the importance of these organelles, especially in neurons. The maintenance of mitochondrial integrity through different surveillance mechanisms is thus critical for neuron survival. Mitochondria display a wide range of quality control mechanisms, from the molecular to the organellar level. Interestingly, many of these lines of defense have been found to be altered in neurodegenerative diseases such as PD and HD. Current knowledge and further elucidation of the novel pathways that protect the cell through mitochondrial quality control may offer unique opportunities for disease therapy in situations where ongoing mitochondrial damage occurs. In this review, we discuss the involvement of mitochondrial dysfunction in neurodegeneration with a special focus on the recent findings regarding mitochondrial quality control pathways, beyond the classical effects of increased production of reactive oxygen species (ROS) and bioenergetic alterations. We also discuss how disturbances in these processes underlie the pathophysiology of neurodegenerative disorders such as PD and HD.

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Section: Mitochondrial Protein Quality Control: the Guarantee Of Mitomentioning

confidence: 99%

Mitochondrial Quality Control in Neurodegenerative Diseases: Focus on Parkinson's Disease and Huntington's Disease

2018

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“…Overexpression of this protein was noted in the case of liver cancer and lung cancer (Takashima et al, 2003;Linxweiler et al, 2014). HSP60, the mammalian molecular chaperone, has a crucial role in protein homeostasis via regulating protein folding and assembly (Okamoto et al, 2017). The level of HSP60 was found to be increased in ovarian cancer, androgen-independent locally advanced prostate cancer and lung cancer, in which its presence was detected intracellularly, pericellularly and also in circulation (Castilla et al, 2010;Bodzek et al, 2014;Agababaoglu et al, 2017).…”

Section: Discussionmentioning

confidence: 99%

Heat shock protein 60 is a disease-associated sialoglycoprotein in human non-small cell lung cancer

Singh

Kumari

Bal

et al. 2020

Biological Chemistry

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The diagnostic and therapeutic potential of Maackia amurensis agglutinin (MAA) have been reported in various malignancies. Earlier, we have found that MAA specifically interacted with human non-small cell lung-cancer (NSCLC) cells and induced apoptosis in these cells. The present study was designed to identify M. amurensis leukoagglutinin (MAL-I, one of the components of MAA, having the same carbohydrate specificity as MAA) interacting membrane sialoglycoprotein(s) of two subtypes of human NSCLC cell lines. Nine proteins were identified using two-dimensional (2D)-polyacrylamide gel electrophoresis (PAGE) followed by MAL-I-overlay transblotting and matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS). Among these proteins, HSP60 was selected for further characterization. The sialoglycoprotein nature of membrane-HSP60 of NSCLC cell lines was confirmed by its reduced reactivity with MAL-I in Western blots in the presence of GM2 and by dual staining of the cell lines with MAL-I and HSP60-antibody. These findings were further substantiated by enzymatic analysis of membrane-HSP60 as well as in-silico evidence regarding this protein. Our observations were validated by immunohistochemical analysis of both subtypes of NSCLC tissue sections. Membrane-HSP60 was found to be involved in the inhibition of MAL-I-induced morphological alteration of NSCLC cells and also in the proliferation and migration of these cells, indicating the probable role of sialylated membrane-HSP60 in this disease.

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“…HSP60, also known as HSPD1, is a mitochondrial chaperonin, involved in the synthesis and transportation of mitochondrial proteins from the cytoplasm to the mitochondria (Cappello et al, 2008). HSP60 is able to interact with different HSPs, such as HSP10, forming a complex that mediates protein folding (Okamoto et al, 2017), and with mitochondrial HSP70 (HSP70A), also known as mortalin, that have a role in cell proliferation and stress (Wadhwa et al, 2006). Studies shows that HSP60 have an important role in the biology of pluripotent cells.…”

Section: Pn and Heat Shock Chaperones In Pscsmentioning

confidence: 99%

Chaperones and Beyond as Key Players in Pluripotency Maintenance

Fernandes

Iglesia²,

Escobar³

et al. 2019

Front. Cell Dev. Biol.

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Pluripotency is orchestrated by distinct players and chaperones and their partners have emerged as pivotal molecules in proteostasis control to maintain stemness. The proteostasis network consists of diverse interconnected pathways that function dynamically according to the needs of the cell to quality control and maintain protein homeostasis. The proteostasis machinery of pluripotent stem cells (PSCs) is finely adjusted in response to distinct stimuli during cell fate commitment to determine successful organism development. Growing evidence has shown different classes of chaperones regulating crucial cellular processes in PSCs. Histones chaperones promote proper nucleosome assembly and modulate the epigenetic regulation of factors involved in PSCs’ rapid turnover from pluripotency to differentiation. The life cycle of pluripotency proteins from synthesis and folding, transport and degradation is finely regulated by chaperones and co-factors either to maintain the stemness status or to cell fate commitment. Here, we summarize current knowledge of the chaperone network that govern stemness and present the versatile role of chaperones in stem cells resilience. Elucidation of the intricate regulation of pluripotency, dissecting in detail molecular determinants and drivers, is fundamental to understanding the properties of stem cells in order to provide a reliable foundation for biomedical research and regenerative medicine.

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HSP60 possesses a GTPase activity and mediates protein folding with HSP10

Cited by 32 publications

References 26 publications

Mitochondrial Quality Control in Neurodegenerative Diseases: Focus on Parkinson's Disease and Huntington's Disease

Mitochondrial Quality Control in Neurodegenerative Diseases: Focus on Parkinson's Disease and Huntington's Disease

Heat shock protein 60 is a disease-associated sialoglycoprotein in human non-small cell lung cancer

Chaperones and Beyond as Key Players in Pluripotency Maintenance

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