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Article ; Online: Identification of HSPB8 modulators counteracting misfolded protein accumulation in neurodegenerative diseases

Chierichetti, Marta / Cerretani, Mauro / Ciammaichella, Alina / Crippa, Valeria / Rusmini, Paola / Ferrari, Veronica / Tedesco, Barbara / Casarotto, Elena / Cozzi, Marta / Mina, Francesco / Pramaggiore, Paola / Galbiati, Mariarita / Piccolella, Margherita / Bresciani, Alberto / Cristofani, Riccardo / Poletti, Angelo

Life Sciences. 2023 June, v. 322 p.121323-

2023

Abstract: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and ... ...

Abstract	The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and insertion into the autophagosome for clearance. CASA is essential to maintain intracellular proteostasis, especially in heart, muscle, and brain often exposed to various types of cell stresses. In neurons, HSPB8 protects against neurotoxicity caused by misfolded proteins in several models of neurodegenerative diseases; by facilitating autophagy, HSPB8 assists misfolded proteins degradation also counteracting proteasome overwhelming and inhibition. To enhance HSPB8 protective activity, we screened a library of approximately 120,000 small molecules to identify compounds capable of increasing HSPB8 gene transcription, translation, or protein stability. We found 83 active compounds active in preliminary dose-response assays and further classified them in 19 chemical classes by medicinal chemists' visual inspection. Of these 19 prototypes, 14 induced HSPB8 mRNA and protein levels in SH-SY5Y cells. Out of these 14 compounds, 3 successfully reduced the aggregation propensity of a disease-associated mutant misfolded superoxide dismutase 1 (SOD1) protein in a flow cytometry-based aggregation assay (Flow cytometric analysis of Inclusions and Trafficking (FloIT)) and induced the expression (mRNA and protein) of some autophagy receptors. Notably, the 3 hits were inactive in HSPB8-depleted cells, confirming that their protective activity is mediated by and requires HSPB8. These compounds may be highly relevant for a therapeutic approach in several human disorders, including neurodegenerative diseases, in which enhancement of CASA exerts beneficial activities.
Keywords	autophagosomes ; brain ; dose response ; flow cytometry ; heart ; heat shock proteins ; humans ; macroautophagy ; muscles ; mutants ; neurotoxicity ; proteasome endopeptidase complex ; superoxide dismutase ; therapeutics ; transcription (genetics) ; HSPB8 ; cancer ; Neurodegenerative disorders ; Neuromuscular disorders ; Chaperone-assisted selective autophagy ; Proteasome
Language	English
Dates of publication	2023-06
Publishing place	Elsevier Inc.
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.121323
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The Role of HSPB8, a Component of the Chaperone-Assisted Selective Autophagy Machinery, in Cancer.

Cristofani, Riccardo / Piccolella, Margherita / Crippa, Valeria / Tedesco, Barbara / Montagnani Marelli, Marina / Poletti, Angelo / Moretti, Roberta M

Cells

2021 Volume 10, Issue 2

Abstract: The cellular response to cancer-induced stress is one of the major aspects regulating cancer development and progression. The Heat Shock Protein B8 (HSPB8) is a small chaperone involved in chaperone-assisted selective autophagy (CASA). CASA promotes the ... ...

Abstract	The cellular response to cancer-induced stress is one of the major aspects regulating cancer development and progression. The Heat Shock Protein B8 (HSPB8) is a small chaperone involved in chaperone-assisted selective autophagy (CASA). CASA promotes the selective degradation of proteins to counteract cell stress such as tumor-induced stress. HSPB8 is also involved in (i) the cell division machinery regulating chromosome segregation and cell cycle arrest in the G0/G1 phase and (ii) inflammation regulating dendritic cell maturation and cytokine production. HSPB8 expression and role are tumor-specific, showing a dual and opposite role. Interestingly, HSPB8 may be involved in the acquisition of chemoresistance to drugs. Despite the fact the mechanisms of HSPB8-mediated CASA activation in tumors need further studies, HSPB8 could represent an important factor in cancer induction and progression and it may be a potential target for anticancer treatment in specific types of cancer. In this review, we will discuss the molecular mechanism underlying HSPB8 roles in normal and cancer conditions. The basic mechanisms involved in anti- and pro-tumoral activities of HSPB8 are deeply discussed together with the pathways that modulate HSPB8 expression, in order to outline molecules with a beneficial effect for cancer cell growth, migration, and death.
MeSH term(s)	Autophagy ; Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/metabolism ; Neoplasms/genetics ; Neoplasms/pathology
Chemical Substances	HSPB8 protein, human ; Heat-Shock Proteins ; Molecular Chaperones
Language	English
Publishing date	2021-02-05
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10020335
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Article ; Online: The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.

Tedesco, Barbara / Ferrari, Veronica / Cozzi, Marta / Chierichetti, Marta / Casarotto, Elena / Pramaggiore, Paola / Mina, Francesco / Galbiati, Mariarita / Rusmini, Paola / Crippa, Valeria / Cristofani, Riccardo / Poletti, Angelo

International journal of molecular sciences

2022 Volume 23, Issue 19

Abstract: Motoneuron diseases (MNDs) are neurodegenerative conditions associated with death of upper and/or lower motoneurons (MNs). Proteostasis alteration is a pathogenic mechanism involved in many MNDs and is due to the excessive presence of misfolded and ... ...

Abstract	Motoneuron diseases (MNDs) are neurodegenerative conditions associated with death of upper and/or lower motoneurons (MNs). Proteostasis alteration is a pathogenic mechanism involved in many MNDs and is due to the excessive presence of misfolded and aggregated proteins. Protein misfolding may be the product of gene mutations, or due to defects in the translation process, or to stress agents; all these conditions may alter the native conformation of proteins making them prone to aggregate. Alternatively, mutations in members of the protein quality control (PQC) system may determine a loss of function of the proteostasis network. This causes an impairment in the capability to handle and remove aberrant or damaged proteins. The PQC system consists of the degradative pathways, which are the autophagy and the proteasome, and a network of chaperones and co-chaperones. Among these components, Heat Shock Protein 70 represents the main factor in substrate triage to folding, refolding, or degradation, and it is assisted in this task by a subclass of the chaperone network, the small heat shock protein (sHSPs/HSPBs) family. HSPBs take part in proteostasis by bridging misfolded and aggregated proteins to the HSP70 machinery and to the degradative pathways, facilitating refolding or clearance of the potentially toxic proteins. Because of its activity against proteostasis alteration, the chaperone system plays a relevant role in the protection against proteotoxicity in MNDs. Here, we discuss the role of HSPBs in MNDs and which HSPBs may represent a valid target for therapeutic purposes.
MeSH term(s)	HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Motor Neuron Disease/metabolism ; Motor Neurons/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding ; Proteostasis Deficiencies/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Heat-Shock Proteins, Small ; Molecular Chaperones ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-10-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms231911759
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Article ; Online: Valosin Containing Protein (VCP): A Multistep Regulator of Autophagy.

Ferrari, Veronica / Cristofani, Riccardo / Tedesco, Barbara / Crippa, Valeria / Chierichetti, Marta / Casarotto, Elena / Cozzi, Marta / Mina, Francesco / Piccolella, Margherita / Galbiati, Mariarita / Rusmini, Paola / Poletti, Angelo

International journal of molecular sciences

2022 Volume 23, Issue 4

Abstract: Valosin containing protein (VCP) has emerged as a central protein in the regulation of the protein quality control (PQC) system. ...

Abstract	Valosin containing protein (VCP) has emerged as a central protein in the regulation of the protein quality control (PQC) system.
MeSH term(s)	Animals ; Autophagy/physiology ; Humans ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism ; Proteostasis/physiology ; Valosin Containing Protein/metabolism
Chemical Substances	Valosin Containing Protein (EC 3.6.4.6)
Language	English
Publishing date	2022-02-09
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23041939
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Article ; Online: The role of autophagy-lysosomal pathway in motor neuron diseases.

Tedesco, Barbara / Ferrari, Veronica / Cozzi, Marta / Chierichetti, Marta / Casarotto, Elena / Pramaggiore, Paola / Mina, Francesco / Piccolella, Margherita / Cristofani, Riccardo / Crippa, Valeria / Rusmini, Paola / Galbiati, Mariarita / Poletti, Angelo

Biochemical Society transactions

2022 Volume 50, Issue 5, Page(s) 1489–1503

Abstract: Motor neuron diseases (MNDs) include a broad group of diseases in which neurodegeneration mainly affects upper and/or lower motor neurons (MNs). Although the involvement of specific MNs, symptoms, age of onset, and progression differ in MNDs, the main ... ...

Abstract	Motor neuron diseases (MNDs) include a broad group of diseases in which neurodegeneration mainly affects upper and/or lower motor neurons (MNs). Although the involvement of specific MNs, symptoms, age of onset, and progression differ in MNDs, the main pathogenic mechanism common to most MNDs is represented by proteostasis alteration and proteotoxicity. This pathomechanism may be directly related to mutations in genes encoding proteins involved in the protein quality control system, particularly the autophagy-lysosomal pathway (ALP). Alternatively, proteostasis alteration can be caused by aberrant proteins that tend to misfold and to aggregate, two related processes that, over time, cannot be properly handled by the ALP. Here, we summarize the main ALP features, focusing on different routes utilized to deliver substrates to the lysosome and how the various ALP pathways intersect with the intracellular trafficking of membranes and vesicles. Next, we provide an overview of the mutated genes that have been found associated with MNDs, how these gene products are involved in different steps of ALP and related processes. Finally, we discuss how autophagy can be considered a valid therapeutic target for MNDs treatment focusing on traditional autophagy modulators and on emerging approaches to overcome their limitations.
MeSH term(s)	Humans ; Autophagy/physiology ; Lysosomes/metabolism ; Motor Neuron Disease/genetics ; Motor Neuron Disease/metabolism ; Proteostasis
Language	English
Publishing date	2022-09-29
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20220778
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Article ; Online: RNA Molecular Signature Profiling in PBMCs of Sporadic ALS Patients: HSP70 Overexpression Is Associated with Nuclear SOD1.

Garofalo, Maria / Pandini, Cecilia / Bordoni, Matteo / Jacchetti, Emanuela / Diamanti, Luca / Carelli, Stephana / Raimondi, Manuela Teresa / Sproviero, Daisy / Crippa, Valeria / Carra, Serena / Poletti, Angelo / Pansarasa, Orietta / Gagliardi, Stella / Cereda, Cristina

Cells

2022 Volume 11, Issue 2

Abstract: Superoxide dismutase 1 (SOD1) is one of the causative genes associated with amyotrophic lateral sclerosis (ALS), a neurodegenerative disorder. SOD1 aggregation contributes to ALS pathogenesis. A fraction of the protein is localized in the nucleus (nSOD1), ...

Abstract	Superoxide dismutase 1 (SOD1) is one of the causative genes associated with amyotrophic lateral sclerosis (ALS), a neurodegenerative disorder. SOD1 aggregation contributes to ALS pathogenesis. A fraction of the protein is localized in the nucleus (nSOD1), where it seems to be involved in the regulation of genes participating in the oxidative stress response and DNA repair. Peripheral blood mononuclear cells (PBMCs) were collected from sporadic ALS (sALS) patients (
MeSH term(s)	Amyotrophic Lateral Sclerosis/blood ; Amyotrophic Lateral Sclerosis/genetics ; Case-Control Studies ; Cell Nucleus/enzymology ; DNA Damage/genetics ; Gene Expression Profiling ; Gene Expression Regulation ; Gene Ontology ; HSP70 Heat-Shock Proteins/metabolism ; Histones/metabolism ; Humans ; Leukocytes, Mononuclear/metabolism ; Methylation ; Principal Component Analysis ; RNA/genetics ; RNA/metabolism ; Superoxide Dismutase-1/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Histones ; RNA (63231-63-0) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2022-01-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11020293
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Article ; Online: Identification of HSPB8 modulators counteracting misfolded protein accumulation in neurodegenerative diseases.

Life sciences

2022 Volume 322, Page(s) 121323

Abstract: Aims: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and ... ...

Abstract	Aims: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and insertion into the autophagosome for clearance. CASA is essential to maintain intracellular proteostasis, especially in heart, muscle, and brain often exposed to various types of cell stresses. In neurons, HSPB8 protects against neurotoxicity caused by misfolded proteins in several models of neurodegenerative diseases; by facilitating autophagy, HSPB8 assists misfolded proteins degradation also counteracting proteasome overwhelming and inhibition. Materials and methods: To enhance HSPB8 protective activity, we screened a library of approximately 120,000 small molecules to identify compounds capable of increasing HSPB8 gene transcription, translation, or protein stability. Key findings: We found 83 active compounds active in preliminary dose-response assays and further classified them in 19 chemical classes by medicinal chemists' visual inspection. Of these 19 prototypes, 14 induced HSPB8 mRNA and protein levels in SH-SY5Y cells. Out of these 14 compounds, 3 successfully reduced the aggregation propensity of a disease-associated mutant misfolded superoxide dismutase 1 (SOD1) protein in a flow cytometry-based aggregation assay (Flow cytometric analysis of Inclusions and Trafficking (FloIT)) and induced the expression (mRNA and protein) of some autophagy receptors. Notably, the 3 hits were inactive in HSPB8-depleted cells, confirming that their protective activity is mediated by and requires HSPB8. Significance: These compounds may be highly relevant for a therapeutic approach in several human disorders, including neurodegenerative diseases, in which enhancement of CASA exerts beneficial activities.
MeSH term(s)	Humans ; Autophagy/physiology ; Heat-Shock Proteins/metabolism ; Molecular Chaperones/metabolism ; Motor Neurons/metabolism ; Neuroblastoma/metabolism ; Neurodegenerative Diseases/metabolism ; Protein Folding
Chemical Substances	Heat-Shock Proteins ; HSPB8 protein, human ; Molecular Chaperones
Language	English
Publishing date	2022-12-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.121323
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Article ; Online: BAG3 Pro209 mutants associated with myopathy and neuropathy relocate chaperones of the CASA-complex to aggresomes.

Adriaenssens, Elias / Tedesco, Barbara / Mediani, Laura / Asselbergh, Bob / Crippa, Valeria / Antoniani, Francesco / Carra, Serena / Poletti, Angelo / Timmerman, Vincent

Scientific reports

2020 Volume 10, Issue 1, Page(s) 8755

Abstract: Three missense mutations targeting the same proline 209 (Pro209) codon in the co-chaperone Bcl2-associated athanogene 3 (BAG3) have been reported to cause distal myopathy, dilated cardiomyopathy or Charcot-Marie-Tooth type 2 neuropathy. Yet, it is ... ...

Abstract	Three missense mutations targeting the same proline 209 (Pro209) codon in the co-chaperone Bcl2-associated athanogene 3 (BAG3) have been reported to cause distal myopathy, dilated cardiomyopathy or Charcot-Marie-Tooth type 2 neuropathy. Yet, it is unclear whether distinct molecular mechanisms underlie the variable clinical spectrum of the rare patients carrying these three heterozygous Pro209 mutations in BAG3. Here, we studied all three variants and compared them to the BAG3_Glu455Lys mutant, which causes dilated cardiomyopathy. We found that all BAG3_Pro209 mutants have acquired a toxic gain-of-function, which causes these variants to accumulate in the form of insoluble HDAC6- and vimentin-positive aggresomes. The aggresomes formed by mutant BAG3 led to a relocation of other chaperones such as HSPB8 and Hsp70, which, together with BAG3, promote the so-called chaperone-assisted selective autophagy (CASA). As a consequence of their increased aggregation-proneness, mutant BAG3 trapped ubiquitinylated client proteins at the aggresome, preventing their efficient clearance. Combined, these data show that all BAG3_Pro209 mutants, irrespective of their different clinical phenotypes, are characterized by a gain-of-function that contributes to the gradual loss of protein homeostasis.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Apoptosis Regulatory Proteins/genetics ; Autophagy ; Cardiomyopathy, Dilated/genetics ; Charcot-Marie-Tooth Disease/genetics ; Codon ; Distal Myopathies/genetics ; HEK293 Cells ; Humans ; Molecular Chaperones/metabolism ; Mutation, Missense ; Proline ; Protein Aggregates ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/metabolism ; Protein Transport ; Ubiquitination
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; BAG3 protein, human ; Codon ; Molecular Chaperones ; Protein Aggregates ; Proline (9DLQ4CIU6V)
Language	English
Publishing date	2020-05-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-65664-z
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Article ; Online: Bicalutamide and Trehalose Ameliorate Spinal and Bulbar Muscular Atrophy Pathology in Mice.

Galbiati, Mariarita / Meroni, Marco / Boido, Marina / Cescon, Matilde / Rusmini, Paola / Crippa, Valeria / Cristofani, Riccardo / Piccolella, Margherita / Ferrari, Veronica / Tedesco, Barbara / Casarotto, Elena / Chierichetti, Marta / Cozzi, Marta / Mina, Francesco / Cicardi, Maria Elena / Pedretti, Silvia / Mitro, Nico / Caretto, Anna / Risè, Patrizia /

Sala, Angelo / Lieberman, Andrew P / Bonaldo, Paolo / Pennuto, Maria / Vercelli, Alessandro / Poletti, Angelo

Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

2023 Volume 20, Issue 2, Page(s) 524–545

Abstract: Spinal and bulbar muscular atrophy (SBMA) is characterized by motor neuron (MN) degeneration that leads to slowly progressive muscle weakness. It is considered a neuromuscular disease since muscle has a primary role in disease onset and progression. SBMA ...

Abstract	Spinal and bulbar muscular atrophy (SBMA) is characterized by motor neuron (MN) degeneration that leads to slowly progressive muscle weakness. It is considered a neuromuscular disease since muscle has a primary role in disease onset and progression. SBMA is caused by a CAG triplet repeat expansion in the androgen receptor (AR) gene. The translated poly-glutamine (polyQ) tract confers a toxic gain of function to the mutant AR altering its folding, causing its aggregation into intracellular inclusions, and impairing the autophagic flux. In an in vitro SBMA neuronal model, we previously showed that the antiandrogen bicalutamide and trehalose, a natural disaccharide stimulating autophagy, block ARpolyQ activation, reduce its nuclear translocation and toxicity and facilitate the autophagic degradation of cytoplasmic AR aggregates. Here, in a knock-in SBMA mouse model (KI AR113Q), we show that bicalutamide and trehalose ameliorated SBMA pathology. Bicalutamide reversed the formation of the AR insoluble forms in KI AR113Q muscle, preventing autophagic flux blockage. We demonstrated that apoptosis is activated in KI AR113Q muscle, and that both compounds prevented its activation. We detected a decrease of mtDNA and an increase of OXPHOS enzymes, already at early symptomatic stages; these alterations were reverted by trehalose. Overall, bicalutamide and/or trehalose led to a partial recovery of muscle morphology and function, and improved SBMA mouse motor behavior, inducing an extension of their survival. Thus, bicalutamide and trehalose, by counteracting ARpolyQ toxicity in skeletal muscle, are valuable candidates for future clinical trials in SBMA patients.
MeSH term(s)	Mice ; Animals ; Bulbo-Spinal Atrophy, X-Linked/drug therapy ; Bulbo-Spinal Atrophy, X-Linked/genetics ; Trehalose/pharmacology ; Trehalose/therapeutic use ; Receptors, Androgen/genetics ; Muscular Atrophy, Spinal ; Anilides/pharmacology ; Mice, Transgenic
Chemical Substances	bicalutamide (A0Z3NAU9DP) ; Trehalose (B8WCK70T7I) ; Receptors, Androgen ; Anilides
Language	English
Publishing date	2023-01-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2316693-9
ISSN	1878-7479 ; 1933-7213
ISSN (online)	1878-7479
ISSN	1933-7213
DOI	10.1007/s13311-023-01343-x
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Article ; Online: HSPB8 frameshift mutant aggregates weaken chaperone-assisted selective autophagy in neuromyopathies.

Tedesco, Barbara / Vendredy, Leen / Adriaenssens, Elias / Cozzi, Marta / Asselbergh, Bob / Crippa, Valeria / Cristofani, Riccardo / Rusmini, Paola / Ferrari, Veronica / Casarotto, Elena / Chierichetti, Marta / Mina, Francesco / Pramaggiore, Paola / Galbiati, Mariarita / Piccolella, Margherita / Baets, Jonathan / Baeke, Femke / De Rycke, Riet / Mouly, Vincent /

Laurenzi, Tommaso / Eberini, Ivano / Vihola, Anna / Udd, Bjarne / Weiss, Lan / Kimonis, Virginia / Timmerman, Vincent / Poletti, Angelo

Autophagy

2023 Volume 19, Issue 8, Page(s) 2217–2239

Abstract: Chaperone-assisted selective autophagy (CASA) is a highly selective pathway for the disposal of misfolding and aggregating proteins. In muscle, CASA assures muscle integrity by favoring the turnover of structural components damaged by mechanical strain. ... ...

Abstract	Chaperone-assisted selective autophagy (CASA) is a highly selective pathway for the disposal of misfolding and aggregating proteins. In muscle, CASA assures muscle integrity by favoring the turnover of structural components damaged by mechanical strain. In neurons, CASA promotes the removal of aggregating substrates. A crucial player of CASA is HSPB8 (heat shock protein family B (small) member 8), which acts in a complex with HSPA, their cochaperone BAG3, and the E3 ubiquitin ligase STUB1. Recently, four novel
MeSH term(s)	Humans ; Sequestosome-1 Protein/genetics ; Sequestosome-1 Protein/metabolism ; Autophagy/genetics ; Heat-Shock Proteins/metabolism ; Neuromuscular Diseases ; Charcot-Marie-Tooth Disease/genetics ; Ubiquitin-Protein Ligases/metabolism ; Adaptor Proteins, Signal Transducing/metabolism ; Apoptosis Regulatory Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism
Chemical Substances	Sequestosome-1 Protein ; Heat-Shock Proteins ; STUB1 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; BAG3 protein, human ; Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; HSPB8 protein, human ; Molecular Chaperones
Language	English
Publishing date	2023-02-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2023.2179780
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