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Evolution and Function of the Hsp70 and Hsp90 Chaperone Machineries...
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Evolution and Function of the Hsp70 and Hsp90 Chaperone Machineries 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (28 January 2023) | Viewed by 11109

Special Issue Editor

Dr. Nikolas Nikolaidis

E-Mail Website
Guest Editor
Department of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA
Interests: heat-shock response; membrane-associated heat-shock proteins; protein–lipid interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Molecular chaperones and in particular the 70 and 90kDa heat-shock proteins (Hsp70s and Hsp90s) play critical roles in cellular and organismal response to stress and survival. At the cellular lever these proteins work in concert with several other helper molecules to form chaperone machines that regulate proteostasis, apoptosis, and cell signaling. This special issue aims to augment our knowledge on the plethora of functional attributes of these molecular machines, their evolution between and within species, as well as how they affect the process of evolution at the cellular and organismal levels.

Prof. Dr. Nikolas Nikolaidis
Guest Editor

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Keywords

  • heat-shock response
  • protein–lipid interactions
  • heat-shock proteins
  • molecular chaperones
  • co-chaperones
  • proteostasis
  • cell signaling
  • stress response
  • adaptation
  • disease

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Published Papers (3 papers)

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Review

22 pages, 1939 KiB  
Review
Role of Ganetespib, an HSP90 Inhibitor, in Cancer Therapy: From Molecular Mechanisms to Clinical Practice
by Mahmoud E. Youssef, Simona Cavalu, Alexandru Madalin Hasan, Galal Yahya, Marwa A. Abd-Eldayem and Sameh Saber
Int. J. Mol. Sci. 2023, 24(5), 5014; https://doi.org/10.3390/ijms24055014 - 6 Mar 2023
Cited by 24 | Viewed by 4433
Abstract
Heat-shock proteins are upregulated in cancer and protect several client proteins from degradation. Therefore, they contribute to tumorigenesis and cancer metastasis by reducing apoptosis and enhancing cell survival and proliferation. These client proteins include the estrogen receptor (ER), epidermal growth factor receptor (EGFR), [...] Read more.
Heat-shock proteins are upregulated in cancer and protect several client proteins from degradation. Therefore, they contribute to tumorigenesis and cancer metastasis by reducing apoptosis and enhancing cell survival and proliferation. These client proteins include the estrogen receptor (ER), epidermal growth factor receptor (EGFR), insulin-like growth factor-1 receptor (IGF-1R), human epidermal growth factor receptor 2 (HER-2), and cytokine receptors. The diminution of the degradation of these client proteins activates different signaling pathways, such as the PI3K/Akt/NF-κB, Raf/MEK/ERK, and JAK/STAT3 pathways. These pathways contribute to hallmarks of cancer, such as self-sufficiency in growth signaling, an insensitivity to anti-growth signals, the evasion of apoptosis, persistent angiogenesis, tissue invasion and metastasis, and an unbounded capacity for replication. However, the inhibition of HSP90 activity by ganetespib is believed to be a promising strategy in the treatment of cancer because of its low adverse effects compared to other HSP90 inhibitors. Ganetespib is a potential cancer therapy that has shown promise in preclinical tests against various cancers, including lung cancer, prostate cancer, and leukemia. It has also shown strong activity toward breast cancer, non-small cell lung cancer, gastric cancer, and acute myeloid leukemia. Ganetespib has been found to cause apoptosis and growth arrest in these cancer cells, and it is being tested in phase II clinical trials as a first-line therapy for metastatic breast cancer. In this review, we will highlight the mechanism of action of ganetespib and its role in treating cancer based on recent studies. Full article
(This article belongs to the Special Issue Evolution and Function of the Hsp70 and Hsp90 Chaperone Machineries 2.0)
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20 pages, 2382 KiB  
Review
Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond
by Shu-ou Shan
Int. J. Mol. Sci. 2023, 24(2), 1170; https://doi.org/10.3390/ijms24021170 - 6 Jan 2023
Cited by 5 | Viewed by 3110
Abstract
The Hsp70 family of molecular chaperones acts as a central ‘hub’ in the cell that interacts with numerous newly synthesized proteins to assist in their biogenesis. Apart from its central and well-established role in facilitating protein folding, Hsp70s also act as key decision [...] Read more.
The Hsp70 family of molecular chaperones acts as a central ‘hub’ in the cell that interacts with numerous newly synthesized proteins to assist in their biogenesis. Apart from its central and well-established role in facilitating protein folding, Hsp70s also act as key decision points in the cellular chaperone network that direct client proteins to distinct biogenesis and quality control pathways. In this paper, we review accumulating data that illustrate a new branch in the Hsp70 network: the post-translational targeting of nascent membrane and organellar proteins to diverse cellular organelles. Work in multiple pathways suggests that Hsp70, via its ability to interact with components of protein targeting and translocation machineries, can initiate elaborate substrate relays in a sophisticated cascade of chaperones, cochaperones, and receptor proteins, and thus provide a mechanism to safeguard and deliver nascent membrane proteins to the correct cellular membrane. We discuss the mechanistic principles gleaned from better-studied Hsp70-dependent targeting pathways and outline the observations and outstanding questions in less well-studied systems. Full article
(This article belongs to the Special Issue Evolution and Function of the Hsp70 and Hsp90 Chaperone Machineries 2.0)
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34 pages, 1491 KiB  
Review
Heat Shock Transcription Factor 2 Is Significantly Involved in Neurodegenerative Diseases, Inflammatory Bowel Disease, Cancer, Male Infertility, and Fetal Alcohol Spectrum Disorder: The Novel Mechanisms of Several Severe Diseases
by Yasuko Tokunaga, Ken-Ichiro Otsuyama, Shigeru Kakuta and Naoki Hayashida
Int. J. Mol. Sci. 2022, 23(22), 13763; https://doi.org/10.3390/ijms232213763 - 9 Nov 2022
Cited by 2 | Viewed by 2878
Abstract
HSF (heat shock transcription factor or heat shock factor) was discovered as a transcription factor indispensable for heat shock response. Although four classical HSFs were discovered in mammals and two major HSFs, HSF1 and HSF2, were cloned in the same year of 1991, [...] Read more.
HSF (heat shock transcription factor or heat shock factor) was discovered as a transcription factor indispensable for heat shock response. Although four classical HSFs were discovered in mammals and two major HSFs, HSF1 and HSF2, were cloned in the same year of 1991, only HSF1 was intensively studied because HSF1 can give rise to heat shock response through the induction of various HSPs’ expression. On the other hand, HSF2 was not well studied for some time, which was probably due to an underestimate of HSF2 itself. Since the beginning of the 21st century, HSF2 research has progressed and many biologically significant functions of HSF2 have been revealed. For example, the roles of HSF2 in nervous system protection, inflammation, maintenance of mitosis and meiosis, and cancer cell survival and death have been gradually unveiled. However, we feel that the fact HSF2 has a relationship with various factors is not yet widely recognized; therefore, the biological significance of HSF2 has been underestimated. We strongly hope to widely communicate the significance of HSF2 to researchers and readers in broad research fields through this review. In addition, we also hope that many readers will have great interest in the molecular mechanism in which HSF2 acts as an active transcription factor and gene bookmarking mechanism of HSF2 during cell cycle progression, as is summarized in this review. Full article
(This article belongs to the Special Issue Evolution and Function of the Hsp70 and Hsp90 Chaperone Machineries 2.0)
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