title: Hsp90 regulates autophagy and plays a role in cancer therapy.
abstract: Nowadays, heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, has become the target of antitumor drugs as a result of its close relationship with the occurrence and development, biological behavior, and prognosis of a tumor. Autophagy has attracted big attention recently for its paradoxical roles in cell survival and cell death, especially in the pathogenesis and treatment of cancer. Moreover, it has been verified that Hsp90 plays a role in autophagy via regulating the stability and activity of signaling proteins, and some Hsp90 inhibitors can induce autophagy. However, the underlying mechanisms for these important processes have not been clarified so far. In this study, we focus on the roles of Hsp90 in the regulation of autophagy, such as toll-like receptor (TLR)-mediated autophagy, Ulk1-mediated mitophagy, and chaperone-mediated autophagy (CMA). The roles of Hsp90 inhibitors in cancer therapy will also be elucidated.
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.
authors.forename: Benli
authors.initials: B
authors.lastname: Wang
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.
authors.forename: Zongyan
authors.initials: Z
authors.lastname: Chen
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.
authors.forename: Feifei
authors.initials: F
authors.lastname: Yu
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.
authors.forename: Qiao
authors.initials: Q
authors.lastname: Chen
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.
authors.forename: Yuxi
authors.initials: Y
authors.lastname: Tian
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China.|Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, MB, R3T 3T2, Canada.
authors.forename: Shumei
authors.initials: S
authors.lastname: Ma
authors.affiliation: Department of Radiation Oncology, the 2nd Hospitals Jilin University, Changchun, 130021, China. 827229953@qq.com.
authors.forename: Tiejun
authors.initials: T
authors.lastname: Wang
authors.affiliation: Key Laboratory of Radiobiology (Ministry of Health), School of Public Health, Jilin University, Changchun, 130021, China. liuxd2014@126.com.|Center for Radiological Research, Columbia University, New York, NY, 10032, USA. liuxd2014@126.com.
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Liu
mesh_terms: D000818:Animals; D001343:Autophagy; D000071189:Autophagy-Related Protein-1 Homolog / Q000378:metabolism; D000071186:Beclin-1 / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism; D016923:Cell Death; D002470:Cell Survival; D018833:Chaperonins / Q000378:metabolism; D015972:Gene Expression Regulation, Neoplastic; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D052119:Lysosomal-Associated Membrane Protein 2 / Q000378:metabolism; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism* / Q000628:therapy*; D015398:Signal Transduction; D051193:Toll-Like Receptors / Q000378:metabolism
chemical_list: C491997:BECN1 protein, human; D000071186:Beclin-1; C498362:CDC37 protein, human; D018797:Cell Cycle Proteins; D018841:HSP90 Heat-Shock Proteins; D047908:Intracellular Signaling Peptides and Proteins; C497811:LAMP2 protein, human; D052119:Lysosomal-Associated Membrane Protein 2; D018832:Molecular Chaperones; D051193:Toll-Like Receptors; D000071189:Autophagy-Related Protein-1 Homolog; C484754:ULK1 protein, human; D018833:Chaperonins
keywords: Autophagy; CMA; Hsp90; Hsp90 inhibition; Mitophagy