At the Crossroads of Apoptosis and Autophagy: Multiple Roles of the Co-Chaperone BAG3 in Stress and Therapy Resistance of Cancer

Kögel, Donat; Linder, Benedikt; Brunschweiger, Andreas; Chines, Silvia; Behl, Christian

doi:10.3390/cells9030574

Cited by 50 publications

(49 citation statements)

References 71 publications

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“…Increased BAG3 expression is shared across all cancer types and can create a desirable microenvironment for cancer progression in pancreatic ductal adenocarcinoma, melanomas, lung cancer, breast cancer, and prostate cancer [180]. Since there is a broad involvement for BAG3 in multiple different cancer types, research has focused on BAG3 inhibitors [181]. A BAG3 inhibitor showed promising efficacy in inhibiting cancer cell proliferation in breast cancer, prostate cancer, pancreatic cancer, and lung cancer cell lines [182].…”

Section: Cancermentioning

confidence: 99%

With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Altınok

Sanchez‐Hodge

Stewart

et al. 2021

Cells

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Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintain protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triage, impacting everything from structural proteins to cell signaling mediators. The chaperone/co-chaperone machinery protects against various stressors to ensure cellular function in the face of stress. However, coding mutations, expression changes, and post-translational modifications of the chaperone/co-chaperone machinery can alter the cellular stress response. Importantly, these dysfunctions appear to contribute to numerous human diseases. Therapeutic targeting of chaperones is an attractive but challenging approach due to the vast functions of HSPs, likely contributing to the off-target effects of these therapies. Current efforts focus on targeting co-chaperones to develop precise treatments for numerous diseases caused by defects in protein quality control. This review focuses on the recent developments regarding selected HSP70/HSP90 co-chaperones, with a concentration on cardioprotection, neuroprotection, cancer, and autoimmune diseases. We also discuss therapeutic approaches that highlight both the utility and challenges of targeting co-chaperones.

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Section: Cancermentioning

confidence: 99%

With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Altınok

Sanchez‐Hodge

Stewart

et al. 2021

Cells

View full text Add to dashboard Cite

show abstract

“…Increased BAG3 expression is shared across all cancer types and can create a desirable microenvironment for cancer progression in pancreatic ductal adenocarcinoma, melanomas, lung cancer, breast cancer, and prostate cancer [157]. Since there is a broad involvement for BAG3 in multiple different cancer types, research has focused on BAG3 inhibitors [158]. A BAG3 inhibitor showed promising efficacy in inhibiting cancer cell proliferation in breast cancer, prostate cancer, pancreatic cancer, and lung cancer cell lines [159].…”

Section: Cancermentioning

confidence: 99%

With or Without You: Co-chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Altınok¹,

Sanchez‐Hodge²,

Stewart³

et al. 2021

Preprint

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Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintaining protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triage, impacting everything from structural proteins to cell signaling mediators. The chaperone/co-chaperone machinery protects against various stressors to ensuring cellular function in the face of stress. However, coding mutations, expression changes, and post-translational modifications of the chaperone/co-chaperone machinery can alter the cellular stress response. Importantly, these dysfunctions appear to contribute to numerous human diseases. Therapeutic targeting of chaperones is an attractive but challenging approach due to the vast functions of HSPs, likely contributing to the off-target effects of these therapies. Current efforts focus on targeting co-chaperones to develop precise treatments for numerous diseases caused by defects in protein quality control. This review focuses on the recent developments regarding selected HSP70/HSP90 co-chaperones, focusing on cardioprotection, neuroprotection, and cancer. We also discuss therapeutic approaches that highlight both the utility and challenges of targeting co-chaperones.

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“…Also, BAG3 interacts with HSP70 and LC3 delivering polyubiquitinated proteins to the autophagy pathway. (179).…”

Section: Autophagy In Stress Responses Cancer Progression and Metasmentioning

confidence: 99%

Autophagy Takes Center Stage as a Possible Cancer Hallmark

et al. 2020

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Cancer remains one of the leading causes of death worldwide, despite significant advances in cancer research and improvements in anticancer therapies. One of the major obstacles to curing cancer is the difficulty of achieving the complete annihilation of resistant cancer cells. The resistance of cancer cells may not only be due to intrinsic factors or factors acquired during the evolution of the tumor but may also be caused by chemotherapeutic treatment failure. Conversely, autophagy is a conserved cellular process in which intracellular components, such as damaged organelles, aggregated or misfolded proteins and macromolecules, are degraded or recycled to maintain cellular homeostasis. Importantly, autophagy is an essential mechanism that plays a key role in tumor initiation and progression. Depending on the cellular context and microenvironmental conditions, autophagy acts as a double-edged sword, playing a role in inducing apoptosis or promoting cell survival. In this review, we propose several scenarios in which autophagy could contribute to cell survival or cell death. Moreover, a special focus on novel promising targets and therapeutic strategies based on autophagic resistant cells is presented.

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At the Crossroads of Apoptosis and Autophagy: Multiple Roles of the Co-Chaperone BAG3 in Stress and Therapy Resistance of Cancer

Cited by 50 publications

References 71 publications

With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

With or Without You: Co-chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Autophagy Takes Center Stage as a Possible Cancer Hallmark

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