The regulation of the small heat shock protein B8 in misfolding protein diseases causing motoneuronal and muscle cell death
Open accessAbstract
Misfolding protein diseases are a wide class of disorders in which the aberrantly folded protein aggregates accumulate in affected cells. In the brain and in the skeletal muscle, misfolded protein accumulation induces a variety of cell dysfunctions that frequently lead to cell death. In motoneuron diseases (MNDs), misfolded proteins accumulate primarily in motoneurons, glial cells and/or skeletal muscle cells, altering motor function. The deleterious effects of misfolded proteins can be counteracted by the activity of the protein quality control (PQC) system, composed of chaperone proteins and degradative systems. Here, we focus on a PQC system component: heat shock protein family B (small) member 8 (HSPB8), a chaperone induced by harmful stressful events, including proteotoxicity. In motoneuron and muscle cells, misfolded proteins activate HSPB8 transcription and enhance HSPB8 levels, which contributes to prevent aggregate formation and their harmful effects. HSPB8 acts not only as a chaperone, but also facilitates the autophagy process, to enable the efficient clearance of the misfolded proteins. HSPB8 acts as a dimer bound to the HSP70 co-chaperone BAG3, a scaffold protein that is also capable of binding to HSP70 (associated with the E3-ligase CHIP) and dynein. When this complex is formed, it is transported by dynein to the microtubule organization center (MTOC), where aggresomes are formed. Here, misfolded proteins are engulfed into nascent autophagosomes to be degraded via the chaperone-assisted selective autophagy (CASA). When CASA is insufficient or impaired, HSP70 and CHIP associate with an alternative co-chaperone, BAG1, which routes misfolded proteins to the proteasome for degradation. The finely tuned equilibrium between proteasome and CASA activity is thought to be crucial for maintaining the functional cell homeostasis during proteotoxic stresses, which in turn is essential for cell survival. This fine equilibrium seems to be altered in MNDs, like Amyotrophic lateral sclerosis (ALS) and spinal and bulbar muscular atrophy (SBMA), contributing to the onset and the progression of disease. Here, we will review how misfolded proteins may affect the PQC system and how the proper activity of this system can be restored by boosting or regulating HSPB8 activity, with the aim to ameliorate disease progression in these two fatal MNDs.
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Loss of proteostasis leads to proteome mislocalisation and aggregation, triggers proteotoxic insults and cell death, which adversely impacts the physiological function of skeletal muscle.
“Loss of proteostasis leads to proteome mislocalisation and aggregation, triggers proteotoxic insults and cell death, which further adversely impacts the physiological function of skeletal muscle (53).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [53]
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- Fuchs M. Poirier D. J. Seguin S. J. Lambert H. Carra S. Charette S. J. (2010). Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction. Biochem. J. 425 245– 255. 10.1042/BJ20090907 19845507 · DOI · Paper page
- Lilienbaum A. (2013). Relationship between the proteasomal system and autophagy. Int. J. Biochem. Mol. Biol. 4 1– 26. 23638318 PMC3627065
Cited by
Sorted by citations
Beckers, J., Tharkeshwar, A. K., & Damme, P. V. (2021) · Autophagy · doi:10.1080/15548627.2021.1872189 · Cited by 124 · see citing works
Disease-modifying therapies in amyotrophic lateral sclerosis
Chiò, A., Mazzini, L., & Mora, G. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.107986 · Cited by 114 · see citing works
Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results
Sarparanta, J., Jonson, P. H., Kawan, S., & Udd, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041409 · Cited by 84 · see citing works
Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space
Adriaenssens, E., Asselbergh, B., Rivera-Mejías, P., Bervoets, S., Vendredy, L., Winter, V. D., Spaas, K., Rycke, R. M. D., Isterdael, G. V., Impens, F., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-022-01074-9 · Cited by 80 · see citing works
The Role of HSPB8, a Component of the Chaperone-Assisted Selective Autophagy Machinery, in Cancer
Cristofani, R., Piccolella, M., Crippa, V., Tedesco, B., Marelli, M. M., Poletti, A., & Moretti, R. M. (2021) · Cells · doi:10.3390/cells10020335 · Cited by 56 · see citing works
From mitochondria to sarcopenia: role of 17β-estradiol and testosterone
Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works
“Loss of proteostasis leads to proteome mislocalisation and aggregation, triggers proteotoxic insults and cell death, which further adversely impacts the physiological function of skeletal muscle (53).”
BackgroundValosin Containing Protein (VCP): A Multistep Regulator of Autophagy
Ferrari, V., Cristofani, R., Tedesco, B., Crippa, V., Chierichetti, M., Casarotto, E., Cozzi, M., Mina, F., Piccolella, M., Galbiati, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041939 · Cited by 50 · see citing works
The eIF2α kinase HRI triggers the autophagic clearance of cytosolic protein aggregates
Mukherjee, T., Ramaglia, V., Abdel‐Nour, M., Bianchi, A. A., Tsalikis, J., Chau, H. N., Kalia, S. K., Kalia, L. V., Chen, J.-J., Arnoult, D., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014415 · Cited by 42 · see citing works
The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70
Gonçalves, C. C., Sharon, I., Schmeing, T. M., Ramos, C. H. I., & Young, J. C. (2021) · Scientific Reports · doi:10.1038/s41598-021-96518-x · Cited by 36 · see citing works
ACK1–AR and AR–HOXB13 signaling axes: epigenetic regulation of lethal prostate cancers
Kim, E. H., Cao, D., Mahajan, N. P., Andriole, G. L., & Mahajan, K. N. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa018 · Cited by 36 · see citing works
Ho, P., Hsieh, T., & Tsai, K. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102441 · Cited by 25 · see citing works
den Broek, B. V., Wuyts, C., Sisto, A., Pintelon, I., Timmermans, J., Somers, V. A., Timmerman, V., Hellings, N., & Irobi, J. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00863-x · Cited by 21 · see citing works
A Crucial Role for the Protein Quality Control System in Motor Neuron Diseases
Cristofani, R., Crippa, V., Cicardi, M. E., Tedesco, B., Ferrari, V., Chierichetti, M., Casarotto, E., Piccolella, M., Messi, E., Galbiati, M., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00191 · Cited by 22 · see citing works
Cristofani, R., Piccolella, M., Marelli, M. M., Tedesco, B., Poletti, A., & Moretti, R. M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05365-9 · Cited by 16 · see citing works
A novel deletion in the C-terminal region of HSPB8 in a family with rimmed vacuolar myopathy
Inoue-Shibui, A., Niihori, T., Kobayashi, M., Suzuki, N., Izumi, R., Warita, H., Hara, K., Shirota, M., Funayama, R., Nakayama, K., et al. (2021) · Journal of Human Genetics · doi:10.1038/s10038-021-00916-y · Cited by 14 · see citing works
Chierichetti, M., Cerretani, M., Ciammaichella, A., Crippa, V., Rusmini, P., Ferrari, V., Tedesco, B., Casarotto, E., Cozzi, M., Mina, F., et al. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121323 · Cited by 13 · see citing works
Lei, T., Xiao, Z., Bi, W., Cai, S., Yang, Y., & Du, H. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101769 · Cited by 11 · see citing works
Xie, F., Li, Z., Yang, N., Yang, J., Hua, D., Luo, J., He, T., & Xing, Y. (2022) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.63.6.28 · Cited by 10 · see citing works
Retinoic Acid Downregulates HSPB8 Gene Expression in Human Breast Cancer Cells MCF-7
Piccolella, M., Cristofani, R., Tedesco, B., Chierichetti, M., Ferrari, V., Casarotto, E., Cozzi, M., Crippa, V., Rusmini, P., Galbiati, M., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.652085 · Cited by 10 · see citing works
The role of autophagy-lysosomal pathway in motor neuron diseases
Tedesco, B., Ferrari, V., Cozzi, M., Chierichetti, M., Casarotto, E., Pramaggiore, P., Mina, F., Piccolella, M., Cristofani, R., Crippa, V., et al. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220778 · Cited by 8 · see citing works
Timothy, F. M., & Zininga, T. (2023) · Frontiers in Cell Death · doi:10.3389/fceld.2023.1322780 · Cited by 8 · see citing works
Mufti, K., Córdova‐Delgado, M., Scott, E. N., Trueman, J. N., Lovnicki, J. M., Loucks, C. M., Rassekh, S. R., Ross, C. J., Carleton, B., Groeneweg, G. S. S., et al. (2024) · npj Genomic Medicine · doi:10.1038/s41525-024-00443-7 · Cited by 7 · see citing works
Khalaf, N. B. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1711422 · Cited by 6 · see citing works
Wu, Y., Xiong, F., & Ling, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112836 · Cited by 5 · see citing works
Heat shock protein 22: A new direction for cardiovascular disease (Review)
Chen, Y., Li, M., & Wu, Y. (2025) · Molecular Medicine Reports · doi:10.3892/mmr.2025.13447 · Cited by 5 · see citing works
Hou, M., Yue, M., Han, X., Sun, T., Zhu, Y., Li, Z., Han, J., Zhao, B., Tu, M., & An, Y. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113369 · Cited by 4 · see citing works
Distal hereditary motor neuronopathy as a new phenotype associated with variants in BAG3
de la Hoz, C. P. D. F.-F., Lupo, V., Bermejo‐Guerrero, L., Martín‐Jiménez, P., Hernández‐Laín, A., Olivé, M., Gallardo, E., Esteban‐Pérez, J., Espinós, C., & Domínguez‐González, C. (2023) · Journal of Neurology · doi:10.1007/s00415-023-12039-9 · Cited by 4 · see citing works
Rong, W., Rome, C. P., & Yao, S. (2021) · Cells Tissues Organs · doi:10.1159/000519600 · Cited by 4 · see citing works
Yerabandi, N., Kouznetsova, V. L., Kesari, S., & Tsigelny, I. F. (2022) · Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology / edited by the Gaetano Conte Academy for the study of striated muscle diseases · doi:10.36185/2532-1900-071 · Cited by 2 · see citing works
Ramanan, S., & Johnson, G. V. W. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.18.665492 · Cited by 1 · see citing works
Van den Broek, B., Wuyts, C., Sisto, A., Pintelon, I., Timmermans, J.-P., Somers, V. A., Timmerman, V., Hellings, N., & Irobi, J. (2022) · Figshare · doi:10.6084/m9.figshare.19720103
Van den Broek, B., Wuyts, C., Sisto, A., Pintelon, I., Timmermans, J.-P., Somers, V. A., Timmerman, V., Hellings, N., & Irobi, J. (2022) · Figshare · doi:10.6084/m9.figshare.19720106
HSPB8 regulates CTP synthase filaments to couple nucleotide metabolism and autophagy in tumorsPreprint
Wang, C.-Y., Lin, W.-C., Huang, K.-J., Chakraborty, A., Lin, Y.-T., Hsieh, Y., Chien, K., Ke, P., Huang, W., Cheng, C.-Y., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.10.704981
Ramanan, S., & Johnson, G. V. W. (2026) · Journal of Molecular Neuroscience · doi:10.1007/s12031-026-02514-z
Alanazi, S. M., Al‐kuraishy, H. M., Alexiou, A. T., Papadakis, M., Faheem, S. A., & Batiha, G. E. (2026) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2026.111834
- Authors
- Cristofani, R., Rusmini, P., Galbiati, M., Cicardi, M. E., Ferrari, V., Tedesco, B., Casarotto, E., Chierichetti, M., Messi, E., Piccolella, M., Carra, S., Crippa, V., & Poletti, A.
- Affiliations
- University of Milan (IT)
- University of Modena and Reggio Emilia (IT)
- Corresponding author
- Poletti, Angelo
- ORCID
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2019-08-02
- Volume
- 13
- Pages
- 796-796
- ISSN
- 1662-453X (ISSN-L)
- PMC
- PMC6688727
- OpenAlex
- W2962463215
- Cited by
- 35
- References
- 178
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 4 · 2023: 4 · 2022: 10 · 2021: 6 · 2020: 5
- FWCI
- 0.46
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- IRIS UNIMORE (University of Modena and Reggio Emilia) (submittedVersion, cc-by)
- Funders
- Fondazione Telethon
- Fondazione Cariplo (2014-0686)
- Fondazione Italiana di Ricerca per la Sclerosi Laterale Amiotrofica
- Association Française contre les Myopathies
- Università degli Studi di Milano
- Ministero della Salute
- Agenzia Italiana del Farmaco, Ministero della Salute
- Regione Lombardia
- Ministero dell’Istruzione, dell’Università e della Ricerca (2015LFPNMN)
- European Molecular Biology Organization
- International Brain Research Organization
- EU Joint Programme – Neurodegenerative Disease Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- HSPB8, protein misfolding, protein quality control, molecular chaperones, HSP70, BAG3, BAG-1, CHIP, dynein, aggresomes, chaperone-assisted selective autophagy, proteasome, amyotrophic lateral sclerosis, spinal and bulbar muscular atrophy, motoneuron death, muscle cell death, proteotoxicity, protein aggregation, motor neuron disease
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