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Journal articles on the topic 'BAG3 protein'

Author: Grafiati

Published: 10 March 2023

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1

Myers, Valerie D., Joseph M. McClung, JuFang Wang, Farzaneh G. Tahrir, Manish K. Gupta, Jennifer Gordon, Christopher H. Kontos, Kamel Khalili, Joseph Y. Cheung, and Arthur M. Feldman. "The Multifunctional Protein BAG3." JACC: Basic to Translational Science 3, no. 1 (February 2018): 122–31. http://dx.doi.org/10.1016/j.jacbts.2017.09.009.

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2

Kögel, Donat, Benedikt Linder, Andreas Brunschweiger, Silvia Chines, and Christian Behl. "At the Crossroads of Apoptosis and Autophagy: Multiple Roles of the Co-Chaperone BAG3 in Stress and Therapy Resistance of Cancer." Cells 9, no. 3 (February 28, 2020): 574. http://dx.doi.org/10.3390/cells9030574.

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BAG3, a multifunctional HSP70 co-chaperone and anti-apoptotic protein that interacts with the ATPase domain of HSP70 through its C-terminal BAG domain plays a key physiological role in cellular proteostasis. The HSP70/BAG3 complex determines the levels of a large number of selective client proteins by regulating their turnover via the two major protein degradation pathways, i.e. proteasomal degradation and macroautophagy. On the one hand, BAG3 competes with BAG1 for binding to HSP70, thereby preventing the proteasomal degradation of its client proteins. By functionally interacting with HSP70 and LC3, BAG3 also delivers polyubiquitinated proteins to the autophagy pathway. BAG3 exerts a number of key physiological functions, including an involvement in cellular stress responses, proteostasis, cell death regulation, development, and cytoskeletal dynamics. Conversely, aberrant BAG3 function/expression has pathophysiological relevance correlated to cardiomyopathies, neurodegeneration, and cancer. Evidence obtained in recent years underscores the fact that BAG3 drives several key hallmarks of cancer, including cell adhesion, metastasis, angiogenesis, enhanced autophagic activity, and apoptosis inhibition. This review provides a state-of-the-art overview on the role of BAG3 in stress and therapy resistance of cancer, with a particular focus on BAG3-dependent modulation of apoptotic signaling and autophagic/lysosomal activity.

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3

Hiebel, Christof, Elisabeth Stürner, Meike Hoffmeister, Georg Tascher, Mario Schwarz, Heike Nagel, Christian Behrends, Christian Münch, and Christian Behl. "BAG3 Proteomic Signature under Proteostasis Stress." Cells 9, no. 11 (November 4, 2020): 2416. http://dx.doi.org/10.3390/cells9112416.

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The multifunctional HSP70 co-chaperone BAG3 (BCL-2-associated athanogene 3) represents a key player in the quality control of the cellular proteostasis network. In response to stress, BAG3 specifically targets aggregation-prone proteins to the perinuclear aggresome and promotes their degradation via BAG3-mediated selective macroautophagy. To adapt cellular homeostasis to stress, BAG3 modulates and functions in various cellular processes and signaling pathways. Noteworthy, dysfunction and deregulation of BAG3 and its pathway are pathophysiologically linked to myopathies, cancer, and neurodegenerative disorders. Here, we report a BAG3 proteomic signature under proteostasis stress. To elucidate the dynamic and multifunctional action of BAG3 in response to stress, we established BAG3 interactomes under basal and proteostasis stress conditions by employing affinity purification combined with quantitative mass spectrometry. In addition to the identification of novel potential BAG3 interactors, we defined proteins whose interaction with BAG3 was altered upon stress. By functional annotation and protein-protein interaction enrichment analysis of the identified potential BAG3 interactors, we confirmed the multifunctionality of BAG3 and highlighted its crucial role in diverse cellular signaling pathways and processes, ensuring cellular proteostasis and cell viability. These include protein folding and degradation, gene expression, cytoskeleton dynamics (including cell cycle and transport), as well as granulostasis, in particular.

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4

Han, Ziying, Michael Schwoerer, Philip Hicks, Jingjing Liang, Gordon Ruthel, Corbett Berry, Bruce Freedman, et al. "Host Protein BAG3 is a Negative Regulator of Lassa VLP Egress." Diseases 6, no. 3 (July 13, 2018): 64. http://dx.doi.org/10.3390/diseases6030064.

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Lassa fever virus (LFV) belongs to the Arenaviridae family and can cause acute hemorrhagic fever in humans. The LFV Z protein plays a central role in virion assembly and egress, such that independent expression of LFV Z leads to the production of virus-like particles (VLPs) that mimic egress of infectious virus. LFV Z contains both PTAP and PPPY L-domain motifs that are known to recruit host proteins that are important for mediating efficient virus egress and spread. The viral PPPY motif is known to interact with specific host WW-domain bearing proteins. Here we identified host WW-domain bearing protein BCL2 Associated Athanogene 3 (BAG3) as a LFV Z PPPY interactor using our proline-rich reading array of WW-domain containing mammalian proteins. BAG3 is a stress-induced molecular co-chaperone that functions to regulate cellular protein homeostasis and cell survival via Chaperone-Assisted Selective Autophagy (CASA). Similar to our previously published findings for the VP40 proteins of Ebola and Marburg viruses, our results using VLP budding assays, BAG3 knockout cells, and confocal microscopy indicate that BAG3 is a WW-domain interactor that negatively regulates egress of LFV Z VLPs, rather than promoting VLP release. Our results suggest that CASA and specifically BAG3 may represent a novel host defense mechanism, whereby BAG3 may dampen egress of several hemorrhagic fever viruses by interacting and interfering with the budding function of viral PPxY-containing matrix proteins.

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5

Rauch, Jennifer N., and Jason E. Gestwicki. "Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro." Journal of Biological Chemistry 289, no. 3 (December 5, 2013): 1402–14. http://dx.doi.org/10.1074/jbc.m113.521997.

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Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). There are six BAG family NEFs in humans, and each is thought to link Hsp70 to a distinct cellular pathway. However, little is known about how the NEFs compete for binding to Hsp70 or how they might differentially shape its biochemical activities. Toward these questions, we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 > Hsp105 ≫ BAG2. All of the NEFs competed for binding to Hsp70, and their relative affinity values predicted their potency in nucleotide and peptide release assays. Finally, we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. The activity of the combinations in ATPase and luciferase refolding assays were dependent on the identity and stoichiometry of both the J protein and NEF so that some combinations were potent chaperones, whereas others were inactive. Given the number and diversity of cochaperones in mammals, it is likely that combinatorial assembly could generate a large number of distinct permutations.

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6

Staibano, Stefania, Massimo Mascolo, Maria Di Benedetto, Maria Luisa Vecchione, Gennaro Ilardi, Giuseppe Di Lorenzo, Riccardo Autorino, et al. "BAG3 protein delocalisation in prostate carcinoma." Tumor Biology 31, no. 5 (June 10, 2010): 461–69. http://dx.doi.org/10.1007/s13277-010-0055-3.

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7

Carra, Serena, Samuel J. Seguin, Herman Lambert, and Jacques Landry. "HspB8 Chaperone Activity toward Poly(Q)-containing Proteins Depends on Its Association with Bag3, a Stimulator of Macroautophagy." Journal of Biological Chemistry 283, no. 3 (November 15, 2007): 1437–44. http://dx.doi.org/10.1074/jbc.m706304200.

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Mutations in HspB8, a member of the B group of heat shock proteins (Hsp), have been associated with human neuromuscular disorders. However, the exact function of HspB8 is not yet clear. We previously demonstrated that overexpression of HspB8 in cultured cells prevents the accumulation of aggregation-prone proteins such as the polyglutamine protein Htt43Q. Here we report that HspB8 forms a stable complex with Bag3 in cells and that the formation of this complex is essential for the activity of HspB8. Bag3 overexpression resulted in the accelerated degradation of Htt43Q, whereas Bag3 knockdown prevented HspB8-induced Htt43Q degradation. Additionally, depleting Bag3 caused a reduction in the endogenous levels of LC3-II, a key molecule involved in macroautophagy, whereas overexpressing Bag3 or HspB8 stimulated the formation LC3-II. These results suggested that the HspB8-Bag3 complex might stimulate the degradation of Htt43Q by macroautophagy. This was confirmed by the observation that treatments with macroautophagy inhibitors significantly decreased HspB8- and Bag3-induced degradation of Htt43Q. We conclude that the HspB8 activity is intrinsically dependent on Bag3, a protein that may facilitate the disposal of doomed proteins by stimulating macroautophagy.

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8

Fuchs, Margit, Dominic J. Poirier, Samuel J. Seguin, Herman Lambert, Serena Carra, Steve J. Charette, and Jacques Landry. "Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction." Biochemical Journal 425, no. 1 (December 14, 2009): 245–57. http://dx.doi.org/10.1042/bj20090907.

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The molecular chaperone HspB8 [Hsp (heat-shock protein) B8] is member of the B-group of Hsps. These proteins bind to unfolded or misfolded proteins and protect them from aggregation. HspB8 has been reported to form a stable molecular complex with the chaperone cohort protein Bag3 (Bcl-2-associated athanogene 3). In the present study we identify the binding regions in HspB8 and Bag3 crucial for their interaction. We present evidence that HspB8 binds to Bag3 through the hydrophobic groove formed by its strands β4 and β8, a region previously known to be responsible for the formation and stability of higher-order oligomers of many sHsps (small Hsps). Moreover, we demonstrate that two conserved IPV (Ile-Pro-Val) motifs in Bag3 mediate its binding to HspB8 and that deletion of these motifs suppresses HspB8 chaperone activity towards mutant Htt43Q (huntingtin exon 1 fragment with 43 CAG repeats). In addition, we show that Bag3 can bind to the molecular chaperone HspB6. The interaction between HspB6 and Bag3 requires the same regions that are involved in the HspB8–Bag3 association and HspB6–Bag3 promotes clearance of aggregated Htt43Q. Our findings suggest that the co-chaperone Bag3 might prevent the accumulation of denatured proteins by regulating sHsp activity and by targeting their substrate proteins for degradation. Interestingly, a mutation in one of Bag3 IPV motifs has recently been associated with the development of severe dominant childhood muscular dystrophy, suggesting a possible important physiological role for HspB–Bag3 complexes in this disease.

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9

Fang, Xi, Julius Bogomolovas, Paul Shichao Zhou, Yongxin Mu, Xiaolong Ma, Zee Chen, Lunfeng Zhang, et al. "P209L mutation in Bag3 does not cause cardiomyopathy in mice." American Journal of Physiology-Heart and Circulatory Physiology 316, no. 2 (February 1, 2019): H392—H399. http://dx.doi.org/10.1152/ajpheart.00714.2018.

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Bcl-2-associated athanogene 3 (BAG3) is a cochaperone protein and a central player of the cellular protein quality control system. BAG3 is prominently expressed in the heart and plays an essential role in cardiac protein homeostasis by interacting with chaperone heat shock proteins (HSPs) in large, functionally distinct multichaperone complexes. The BAG3 mutation of proline 209 to leucine (P209L), which resides in a critical region that mediates the direct interaction between BAG3 and small HSPs (sHSPs), is associated with cardiomyopathy in humans. However, the mechanism by which the BAG3 P209L missense mutation leads to cardiomyopathy remains unknown. To determine the molecular basis underlying the cardiomyopathy caused by the BAG3 P209L mutation, we generated a knockin (KI) mouse model in which the endogenous Bag3 gene was replaced with mutant Bag3 containing the P215L mutation, which is equivalent to the human P209L mutation. We performed physiological, histological, and biochemical analyses of Bag3 P209L KI mice to determine the functional, morphological, and molecular consequences of the P209L mutation. We found that Bag3 P209L KI mice exhibited normal cardiac function and morphology up to 16 mo of age. Western blot analysis further revealed that levels of sHSPs, stress-inducible HSPs, ubiquitinated proteins, and autophagy were unaffected in P209L mutant mouse hearts. In conclusion, the P209L mutation in Bag3 does not cause cardiomyopathy in mice up to 16 mo of age under baseline conditions. NEW & NOTEWORTHY Bcl-2-associated athanogene 3 (BAG3) P209L mutation is associated with human cardiomyopathy. A recent study reported that transgenic mice overexpressing human BAG3 P209L in cardiomyocytes have cardiac dysfunction. In contrast, our P209L mice that express mutant BAG3 at the same level as that of wild-type mice displayed no overt phenotype. Our results suggest that human cardiomyopathy may result from species-specific requirements for the conserved motif that is disrupted by P209L mutation or from genetic background-dependent effects.

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10

Kyratsous, Christos A., and Saul J. Silverstein. "BAG3, a Host Cochaperone, Facilitates Varicella-Zoster Virus Replication." Journal of Virology 81, no. 14 (May 2, 2007): 7491–503. http://dx.doi.org/10.1128/jvi.00442-07.

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ABSTRACT Varicella-zoster virus (VZV) establishes a lifelong latent infection in the dorsal root ganglia of the host. During latency, a subset of virus-encoded regulatory proteins is detected; however, they are excluded from the nucleus. ORF29p, a single-stranded DNA binding protein, is one of these latency-associated proteins. We searched for cell proteins that interact with ORF29p and identified BAG3. BAG3, Hsp70/Hsc70, and Hsp90 colocalize with ORF29p in nuclear transcription/replication factories during lytic replication of VZV. Pharmacological intercession of Hsp90 activity with ansamycin antibiotics or depletion of BAG3 by small interfering RNA results in inhibition of virus replication. Replication in BAG3-depleted cell lines is restored by complementation with exogenous BAG3. Alteration of host chaperone activity provides a novel means of regulating virus replication.

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11

Basile, Anna, Nune Darbinian, Rafal Kaminski, Martyn K. White, Antonio Gentilella, Maria Caterina Turco, and Kamel Khalili. "Evidence for modulation of BAG3 by polyomavirus JC early protein." Journal of General Virology 90, no. 7 (July 1, 2009): 1629–40. http://dx.doi.org/10.1099/vir.0.008722-0.

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Polyomavirus JC (JCV) infects oligodendrocytes and astrocytes in the brain and is the cause of the demyelinating disease progressive multifocal leukoencephalopathy (PML). In cell culture, JCV infection is characterized by severe damage to cellular DNA, which begins early in infection, and a viral cytopathic effect, which is observed late in infection. Nevertheless, these JCV-infected cells show a low level of apoptosis, at both the early and late stages of infection. This suggests that there is conflicting interplay between viral anti-apoptotic pathways that seek to optimize virus production, e.g. through T antigen (T-Ag)–p53 interaction, and cellular pro-apoptotic pathways that seek to eliminate virally infected cells. The apoptosis regulatory protein BAG3 is a member of the human Bcl-2-associated athanogene (BAG) family of proteins, which function as molecular co-chaperones through their interaction with Hsc70/Hsp70 and function in the regulation of the cellular stress response, proliferation and apoptosis. This study showed that BAG3 protein is downregulated upon JCV infection and that this effect is mediated by JCV T-Ag via repression of the BAG3 promoter. The site of action of T-Ag was mapped to an AP2 site in the BAG3 promoter, and gel shift and chromatin immunoprecipitation assays showed that T-Ag inhibited AP2 binding to this site, resulting in downregulation of BAG3 promoter expression. Using BAG3 and T-Ag expression and BAG3 siRNA, it was found that BAG3 and T-Ag had antagonistic effects on the induction of apoptosis, being anti-apoptotic and pro-apoptotic, respectively. The significance of these interactions to the JCV life cycle is discussed.

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12

Lyu, Chuang, Wei-Dong Li, Shu-Wen Wang, Jin-Mei Peng, Yong-Bo Yang, Zhi-Jun Tian, and Xue-Hui Cai. "Host BAG3 Is Degraded by Pseudorabies Virus pUL56 C-Terminal 181L-185L and Plays a Negative Regulation Role during Viral Lytic Infection." International Journal of Molecular Sciences 21, no. 9 (April 29, 2020): 3148. http://dx.doi.org/10.3390/ijms21093148.

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Bcl2-associated athanogene (BAG) 3, which is a chaperone-mediated selective autophagy protein, plays a pivotal role in modulating the life cycle of a wide variety of viruses. Both positive and negative modulations of viruses by BAG3 were reported. However, the effects of BAG3 on pseudorabies virus (PRV) remain unknown. To investigate whether BAG3 could modulate the PRV life cycle during a lytic infection, we first identified PRV protein UL56 (pUL56) as a novel BAG3 interactor by co-immunoprecipitation and co-localization analyses. The overexpression of pUL56 induced a significant degradation of BAG3 at protein level via the lysosome pathway. The C-terminal mutations of 181L/A, 185L/A, or 181L/A-185L/A in pUL56 resulted in a deficiency in pUL56-induced BAG3 degradation. In addition, the pUL56 C-terminal mutants that lost Golgi retention abrogated pUL56-induced BAG3 degradation, which indicates a Golgi retention-dependent manner. Strikingly, BAG3 was not observed to be degraded in either wild-type or UL56-deleted PRV infected cells as compared to mock infected ones, whereas the additional two adjacent BAG3 cleaved products were found in the infected cells in a species-specific manner. Overexpression of BAG3 significantly suppressed PRV proliferation, while knockdown of BAG3 resulted in increased viral yields in HEK293T cells. Thus, these data indicated a negative regulation role of BAG3 during PRV lytic infection. Collectively, our findings revealed a novel molecular mechanism on host protein degradation induced by PRV pUL56. Moreover, we identified BAG3 as a host restricted protein during PRV lytic infection in cells.

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13

De Marco, Margot, Raffaella D’Auria, Alessandra Rosati, Gennaro Vitulano, Alberto Gigantino, Rodolfo Citro, Federico Piscione, Jodi Zilinski, James L. Januzzi, and Maria Caterina Turco. "BAG3 Protein in Advanced-Stage Heart Failure." JACC: Heart Failure 2, no. 6 (December 2014): 673–75. http://dx.doi.org/10.1016/j.jchf.2014.05.012.

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14

Marzullo, Liberato, Maria Caterina Turco, and Margot De Marco. "The multiple activities of BAG3 protein: Mechanisms." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 8 (August 2020): 129628. http://dx.doi.org/10.1016/j.bbagen.2020.129628.

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15

McCollum, Andrea K., Giovanna Casagrande, and Elise C. Kohn. "Caught in the middle: the role of Bag3 in disease." Biochemical Journal 425, no. 1 (December 14, 2009): e1-e3. http://dx.doi.org/10.1042/bj20091739.

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Bag3 is a Bag family co-chaperone that regulates the ATPase activity of Hsp70 (heat-shock protein 70) chaperones. Recent studies have demonstrated that Bag3 can initiate macroautophagy in co-operation with small heat-shock protein HspB8. In this issue of the Biochemical Journal, Fuchs and co-workers have discovered the IPV motif in Bag3 that is necessary for binding to HspB8. The authors have also identified HspB6 as a new binding partner for Bag3 and characterized further the binding of both HspB8 and HspB6 in Bag3-mediated clearance of aggregated polyglutamine-containing protein Htt43Q (huntingtin exon 1 fragment with 43 CAG repeats). It is clear from recent identification of a Bag3 mutation that causes a form of muscular dystrophy that the full function of Bag3 in disease is not clear. We will apply the findings of Fuchs et al. in this issue to reconcile the phenotypes of Bag3 homologue knockouts with the emerging role of Bag3 in autophagy.

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16

Rocchi, Angela, Hassen S. Wollebo, and Kamel Khalili. "Protein Quality Control in Glioblastoma: A Review of the Current Literature with New Perspectives on Therapeutic Targets." International Journal of Molecular Sciences 23, no. 17 (August 27, 2022): 9734. http://dx.doi.org/10.3390/ijms23179734.

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Protein quality control allows eukaryotes to maintain proteostasis under the stress of constantly changing conditions. In this review, we discuss the current literature on PQC, highlighting flaws that must exist for malignancy to occur. At the nidus of PQC, the expression of BAG1-6 reflects the cell environment; each isoform directs proteins toward different, parallel branches of the quality control cascade. The sum of these branches creates a net shift toward either homeostasis or apoptosis. With an established role in ALP, Bag3 is necessary for cell survival in stress conditions including those of the cancerous niche (i.e., hypoxia, hypermutation). Evidence suggests that excessive Bag3–HSP70 activity not only sustains, but also propagates cancers. Its role is anti-apoptotic—which allows malignant cells to persist—and intercellular—with the production of infectious ‘oncosomes’ enabling cancer expansion and recurrence. While Bag3 has been identified as a key prognostic indicator in several cancer types, its investigation is limited regarding glioblastoma. The cochaperone HSP70 has been strongly linked with GBM, while ALP inhibitors have been shown to improve GBM susceptibility to chemotherapeutics. Given the highly resilient, frequently recurrent nature of GBM, the targeting of Bag3 is a necessary consideration for the successful and definitive treatment of GBM.

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17

Chiappetta, Gennaro, Massimo Ammirante, Anna Basile, Alessandra Rosati, Michela Festa, Mario Monaco, Emilia Vuttariello, et al. "The Antiapoptotic Protein BAG3 Is Expressed in Thyroid Carcinomas and Modulates Apoptosis Mediated by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand." Journal of Clinical Endocrinology & Metabolism 92, no. 3 (March 1, 2007): 1159–63. http://dx.doi.org/10.1210/jc.2006-1712.

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Abstract Context: We previously showed that BAG3 protein, a member of the BAG (Bcl-2-associated athanogene) co-chaperone family, modulates apoptosis in human leukemias. The expression of BAG3 in other tumor types has not been extensively investigated so far. Objective: The objective of this study was to analyze BAG3 expression in thyroid neoplastic cells and investigate its influence in cell apoptotic response to TNF-related apoptosis-inducing ligand (TRAIL). Design, Setting, and Patients: We investigated BAG3 expression in human thyroid carcinoma cell lines, including NPA, and the effect of BAG3-specific small interfering RNA on TRAIL-induced apoptosis in NPA cells. Subsequently, we analyzed BAG3 expression in 30 benign lesions and 56 carcinomas from patients of the Naples Tumor Institute Fondazione Senatore Pascale. Main Outcome Measures: The main outcome measures were: analysis of BAG3 protein in NPA cells by Western blot and immunocytochemistry; analysis of apoptosis in TRAIL-stimulated NPA cells by flow cytometry; and evaluation of BAG3 expression in specimens from thyroid lesions by immunohistochemistry. Results: BAG3 was expressed in human thyroid carcinoma cell lines; small interfering RNA-mediated downmodulation of its levels significantly (P < 0.0195) enhanced NPA cell apoptotic response to TRAIL. The protein was not detectable in 19 of 20 specimens of normal thyroid or goiters, whereas 54 of 56 analyzed carcinomas (15 follicular, 28 papillary, and 13 anaplastic) were clearly positive for BAG3 expression. Conclusions: BAG3 downmodulates the apoptotic response to TRAIL in human neoplastic thyroid cells. The protein is specifically expressed in thyroid carcinomas and not in normal thyroid tissue or goiter.

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18

Meriin, Anatoli B., Arjun Narayanan, Le Meng, Ilya Alexandrov, Xaralabos Varelas, Ibrahim I. Cissé, and Michael Y. Sherman. "Hsp70–Bag3 complex is a hub for proteotoxicity-induced signaling that controls protein aggregation." Proceedings of the National Academy of Sciences 115, no. 30 (July 9, 2018): E7043—E7052. http://dx.doi.org/10.1073/pnas.1803130115.

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Protein abnormalities in cells are the cause of major pathologies, and a number of adaptive responses have evolved to relieve the toxicity of misfolded polypeptides. To trigger these responses, cells must detect the buildup of aberrant proteins which often associate with proteasome failure, but the sensing mechanism is poorly understood. Here we demonstrate that this mechanism involves the heat shock protein 70–Bcl-2–associated athanogene 3 (Hsp70–Bag3) complex, which upon proteasome suppression responds to the accumulation of defective ribosomal products, preferentially recognizing the stalled polypeptides. Components of the ribosome quality control system LTN1 and VCP and the ribosome-associated chaperone NAC are necessary for the interaction of these species with the Hsp70–Bag3 complex. This complex regulates important signaling pathways, including the Hippo pathway effectors LATS1/2 and the p38 and JNK stress kinases. Furthermore, under proteotoxic stress Hsp70–Bag3–LATS1/2 signaling regulates protein aggregation. We established that the regulated step was the emergence and growth of abnormal protein oligomers containing only a few molecules, indicating that aggregation is regulated at very early stages. The Hsp70–Bag3 complex therefore functions as an important signaling node that senses proteotoxicity and triggers multiple pathways that control cell physiology, including activation of protein aggregation.

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Liu, Xia, Toru Yamashita, Jingwei Shang, Xiaowen Shi, Ryuta Morihara, Yong Huang, Kota Sato, et al. "Molecular switching from ubiquitin-proteasome to autophagy pathways in mice stroke model." Journal of Cerebral Blood Flow & Metabolism 40, no. 1 (October 30, 2018): 214–24. http://dx.doi.org/10.1177/0271678x18810617.

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The ubiquitin-proteasome system (UPS) and autophagy are two major pathways to degrade misfolded proteins that accumulate under pathological conditions. When UPS is overloaded, the degeneration pathway may switch to autophagy to remove excessive misfolded proteins. However, it is still unclear whether and how this switch occurs during cerebral ischemia. In the present study, transient middle cerebral artery occlusion (tMCAO) resulted in accelerated ubiquitin-positive protein aggregation from 0.5 h of reperfusion in mice brain after 10, 30 or 60 min of tMCAO. In contrast, significant reduction of p62 and induction of LC3-II were observed, peaking at 24 h of reperfusion after 30 and 60 min tMCAO. Western blot analyses showed an increase of BAG3 and HDAC6 at 1 or 24 h of reperfusion that was dependent on the ischemic period. In contract, BAG1 decreased at 24 h of reperfusion after 10, 30 or 60 min of tMCAO after double immunofluorescent colocalization of ubiquitin, HSP70, p62 and BAG3. These data suggest that a switch from UPS to autophagy occurred between 10 and 30 min of cerebral ischemia depending on the BAG1/BAG3 ratio and level of HDAC6.

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Wang, Yingying, and Yongjie Tian. "miR-206 Inhibits Cell Proliferation, Migration, and Invasion by Targeting BAG3 in Human Cervical Cancer." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 26, no. 6 (July 5, 2018): 923–31. http://dx.doi.org/10.3727/096504017x15143731031009.

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miR-206 and Bcl-2-associated athanogene 3 (BAG3) have been suggested as important regulators in various cancer types. However, the biological role of miR-206 and BAG3 in cervical cancer (CC) remains unclear. We investigated the expressions and mechanisms of miR-206 and BAG3 in CC using in vitro and in vivo assays. In the present study, miR-206 expression was expressed at a lower level in CC tissues and cells than adjacent normal tissues and NEECs. By contrast, BAG3 mRNA and protein were expressed at higher levels in CC tissues and cells. Furthermore, miR-206 overexpression repressed cell proliferation, migration, and invasion in vitro, and the 3′-untranslated region (3′-UTR) of BAG3 was a direct target of miR-206. miR-206 overexpression also inhibited EGFR, Bcl-2, and MMP2/9 protein expression, but promoted Bax protein expression. Besides, BAG3 overexpression partially abrogated miR-206-inhibited cell proliferation and invasion, while BAG3 silencing enhanced miR-206-mediated inhibition. In vivo assay revealed that miR-206 repressed tumor growth in nude mice xenograft model. In conclusion, miR-206 inhibits cell proliferation, migration, and invasion by targeting BAG3 in human CC. Thus, miR-206-BAG3 can be used as a useful target for CC.

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Luthold, Carole, Herman Lambert, Solenn M. Guilbert, Marc-Antoine Rodrigue, Margit Fuchs, Alice-Anaïs Varlet, Amélie Fradet-Turcotte, and Josée N. Lavoie. "CDK1-Mediated Phosphorylation of BAG3 Promotes Mitotic Cell Shape Remodeling and the Molecular Assembly of Mitotic p62 Bodies." Cells 10, no. 10 (October 2, 2021): 2638. http://dx.doi.org/10.3390/cells10102638.

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The cochaperone BCL2-associated athanogene 3 (BAG3), in complex with the heat shock protein HSPB8, facilitates mitotic rounding, spindle orientation, and proper abscission of daughter cells. BAG3 and HSPB8 mitotic functions implicate the sequestosome p62/SQSTM1, suggesting a role for protein quality control. However, the interplay between this chaperone-assisted pathway and the mitotic machinery is not known. Here, we show that BAG3 phosphorylation at the conserved T285 is regulated by CDK1 and activates its function in mitotic cell shape remodeling. BAG3 phosphorylation exhibited a high dynamic at mitotic entry and both a non-phosphorylatable BAG3T285A and a phosphomimetic BAG3T285D protein were unable to correct the mitotic defects in BAG3-depleted HeLa cells. We also demonstrate that BAG3 phosphorylation, HSPB8, and CDK1 activity modulate the molecular assembly of p62/SQSTM1 into mitotic bodies containing K63 polyubiquitinated chains. These findings suggest the existence of a mitotically regulated spatial quality control mechanism for the fidelity of cell shape remodeling in highly dividing cells.

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22

Lee, Jae Chang, Sung Ae Koh, Kyung Hee Lee, and Jae-Ryong Kim. "BAG3 contributes to HGF-mediated cell proliferation, migration, and invasion via the Egr1 pathway in gastric cancer." Tumori Journal 105, no. 1 (December 4, 2018): 63–75. http://dx.doi.org/10.1177/0300891618811274.

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Introduction: Bcl2-associated athanogene 3 (BAG3) is elevated in several types of cancers. However, the role of BAG3 in progression of gastric cancer is unknown. Therefore, the present study aims to find out the role of BAG3 in hepatocyte growth factor (HGF)–mediated tumor progression and the molecular mechanisms by which HGF regulates BAG3 expression. Methods: BAG3 mRNA and protein were measured using reverse transcription polymerase chain reaction and Western blot in the 2 human gastric cancer cell lines, NUGC3 and MKN28, treated with or without HGF. The effects of BAG3 knockdown on cell proliferation, cell invasion, and apoptosis were analyzed by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay, the in vitro 2-chamber invasion assay, and flow cytometry in BAG3 short hairpin RNA (shRNA)–transfected cells and control cells. The signaling pathways involved in BAG3 that are regulated by HGF were analyzed. The chromatin immunoprecipitation assay was used to determine binding of Egr1 to the BAG3 promoter. Results: BAG3 mRNA and protein levels were increased following treatment with HGF. HGF-mediated BAG3 upregulation increased cell proliferation and cell invasion; however, it decreased apoptosis. HGF-mediated BAG3 upregulation is regulated by an ERK and Egr1-dependent pathway. BAG3 may have an important role in HGF-mediated cell proliferation and metastasis in gastric cancer through an ERK and Egr1-dependent pathway. Conclusion: This pathway may provide novel therapeutic targets and provide information for further identification of other targets of therapeutic significance in gastric cancer.

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Sarparanta, Jaakko, Per Harald Jonson, Sabita Kawan, and Bjarne Udd. "Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results." International Journal of Molecular Sciences 21, no. 4 (February 19, 2020): 1409. http://dx.doi.org/10.3390/ijms21041409.

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Skeletal muscle and the nervous system depend on efficient protein quality control, and they express chaperones and cochaperones at high levels to maintain protein homeostasis. Mutations in many of these proteins cause neuromuscular diseases, myopathies, and hereditary motor and sensorimotor neuropathies. In this review, we cover mutations in DNAJB6, DNAJB2, αB-crystallin (CRYAB, HSPB5), HSPB1, HSPB3, HSPB8, and BAG3, and discuss the molecular mechanisms by which they cause neuromuscular disease. In addition, previously unpublished results are presented, showing downstream effects of BAG3 p.P209L on DNAJB6 turnover and localization.

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Ruggiero, Dafne, Stefania Terracciano, Gianluigi Lauro, Michela Pecoraro, Silvia Franceschelli, Giuseppe Bifulco, and Ines Bruno. "Structural Refinement of 2,4-Thiazolidinedione Derivatives as New Anticancer Agents Able to Modulate the BAG3 Protein." Molecules 27, no. 3 (January 20, 2022): 665. http://dx.doi.org/10.3390/molecules27030665.

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The multidomain BAG3 protein is a member of the BAG (Bcl-2-associated athanogene) family of co-chaperones, involved in a wide range of protein–protein interactions crucial for many key cellular pathways, including autophagy, cytoskeletal dynamics, and apoptosis. Basal expression of BAG3 is elevated in several tumor cell lines, where it promotes cell survival signaling and apoptosis resistance through the interaction with many protein partners. In addition, its role as a key player of several hallmarks of cancer, such as metastasis, angiogenesis, autophagy activation, and apoptosis inhibition, has been established. Due to its involvement in malignant transformation, BAG3 has emerged as a potential and effective biological target to control multiple cancer-related signaling pathways. Recently, by using a multidisciplinary approach we reported the first synthetic BAG3 modulator interfering with its BAG domain (BD), based on a 2,4-thiazolidinedione scaffold and endowed with significant anti-proliferative activity. Here, a further in silico-driven selection of a 2,4-thiazolidinedione-based compound was performed. Thanks to a straightforward synthesis, relevant binding affinity for the BAG3BD domain, and attractive biological activities, this novel generation of compounds is of great interest for the development of further BAG3 binders, as well as for the elucidation of the biological roles of this protein in tumors. Specifically, we found compound 6 as a new BAG3 modulator with a relevant antiproliferative effect on two different cancer cell lines (IC50: A375 = 19.36 μM; HeLa = 18.67 μM).

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Rosati, A., V. Graziano, V. De Laurenzi, M. Pascale, and M. C. Turco. "BAG3: a multifaceted protein that regulates major cell pathways." Cell Death & Disease 2, no. 4 (April 2011): e141-e141. http://dx.doi.org/10.1038/cddis.2011.24.

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Bruno, Anna Paola, Michela Festa, Fabrizio Dal Piaz, Alessandra Rosati, Maria Caterina Turco, Antonio Giuditta, and Liberato Marzullo. "Identification of a synaptosome- associated form of BAG3 protein." Cell Cycle 7, no. 19 (October 2008): 3104–5. http://dx.doi.org/10.4161/cc.7.19.6774.

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Romano, M. F., M. Festa, G. Pagliuca, R. Lerose, R. Bisogni, F. Chiurazzi, G. Storti, et al. "BAG3 protein controls B-chronic lymphocytic leukaemia cell apoptosis." Cell Death & Differentiation 10, no. 3 (March 2003): 383–85. http://dx.doi.org/10.1038/sj.cdd.4401167.

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Esposito, Veronica, Carlo Baldi, Pio Zeppa, Michelina Festa, Luana Guerriero, Morena d'Avenia, Massimiliano Chetta, et al. "BAG3 Protein Is Over-Expressed in Endometrioid Endometrial Adenocarcinomas." Journal of Cellular Physiology 232, no. 2 (July 22, 2016): 309–11. http://dx.doi.org/10.1002/jcp.25489.

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Gout, E., M. Gutkowska, S. Takayama, J. C. Reed, and J. Chroboczek. "Co-chaperone BAG3 and adenovirus penton base protein partnership." Journal of Cellular Biochemistry 111, no. 3 (July 6, 2010): 699–708. http://dx.doi.org/10.1002/jcb.22756.

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Franceschelli, Silvia, Anna Paola Bruno, Michela Festa, Antonia Falco, Elisa Gionti, Morena d’Avenia, Margot De Marco, et al. "BAG3 Protein Is Involved in Endothelial Cell Response to Phenethyl Isothiocyanate." Oxidative Medicine and Cellular Longevity 2018 (May 31, 2018): 1–12. http://dx.doi.org/10.1155/2018/5967890.

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Phenethyl isothiocyanate (PEITC), a cruciferous vegetable-derived compound, is a versatile cancer chemopreventive agent that displays the ability to inhibit tumor growth during initiation, promotion, and progression phases in several animal models of carcinogenesis. In this report, we dissect the cellular events induced by noncytotoxic concentrations of PEITC in human umbilical vein endothelial cells (HUVECs). In the early phase, PEITC treatment elicited cells’ morphological changes that comprise reduction in cell volume and modification of actin organization concomitantly with a rapid activation of the PI3K/Akt pathway. Downstream to PI3K, PEITC also induces the activity of Rac1 and activation of c-Jun N-terminal kinase (JNK), well-known regulators of actin cytoskeleton dynamics. Interestingly, PEITC modifications of the actin cytoskeleton were abrogated by pretreatment with JNK inhibitor, SP600125. JNK signaling led also to the activation of the c-Jun transcription factor, which is involved in the upregulation of several genes; among them is the BAG3 protein. This protein, a member of the BAG family of heat shock protein (Hsp) 70 cochaperones, is able to sustain survival in different tumor cell lines and neoangiogenesis by directly regulating the endothelial cell cycle. Furthermore, BAG3 is involved in maintaining actin folding. Our findings indicate that BAG3 protein expression is induced in endothelial cells upon exposure to a noncytotoxic concentration of PEITC and its expression is requested for the recovery of normal cell size and morphology after the stressful stimuli. This assigns an additional role for BAG3 protein in the endothelial cells after a stress event.

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Luthold, Carole, Alice-Anaïs Varlet, Herman Lambert, François Bordeleau, and Josée N. Lavoie. "Chaperone-Assisted Mitotic Actin Remodeling by BAG3 and HSPB8 Involves the Deacetylase HDAC6 and Its Substrate Cortactin." International Journal of Molecular Sciences 22, no. 1 (December 25, 2020): 142. http://dx.doi.org/10.3390/ijms22010142.

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The fidelity of actin dynamics relies on protein quality control, but the underlying molecular mechanisms are poorly defined. During mitosis, the cochaperone BCL2-associated athanogene 3 (BAG3) modulates cell rounding, cortex stability, spindle orientation, and chromosome segregation. Mitotic BAG3 shows enhanced interactions with its preferred chaperone partner HSPB8, the autophagic adaptor p62/SQSTM1, and HDAC6, a deacetylase with cytoskeletal substrates. Here, we show that depletion of BAG3, HSPB8, or p62/SQSTM1 can recapitulate the same inhibition of mitotic cell rounding. Moreover, depletion of either of these proteins also interfered with the dynamic of the subcortical actin cloud that contributes to spindle positioning. These phenotypes were corrected by drugs that limit the Arp2/3 complex or HDAC6 activity, arguing for a role for BAG3 in tuning branched actin network assembly. Mechanistically, we found that cortactin acetylation/deacetylation is mitotically regulated and is correlated with a reduced association of cortactin with HDAC6 in situ. Remarkably, BAG3 depletion hindered the mitotic decrease in cortactin–HDAC6 association. Furthermore, expression of an acetyl-mimic cortactin mutant in BAG3-depleted cells normalized mitotic cell rounding and the subcortical actin cloud organization. Together, these results reinforce a BAG3′s function for accurate mitotic actin remodeling, via tuning cortactin and HDAC6 spatial dynamics.

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Mukhtar, Idris. "Modelling and docking analysis of a tumor target protein BAG3." Bioinformation 16, no. 4 (April 30, 2020): 351–58. http://dx.doi.org/10.6026/97320630016351.

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Carrizzo, Albino, Antonio Damato, Mariateresa Ambrosio, Antonia Falco, Alessandra Rosati, Mario Capunzo, Michele Madonna, et al. "The prosurvival protein BAG3: a new participant in vascular homeostasis." Cell Death & Disease 7, no. 10 (October 2016): e2431-e2431. http://dx.doi.org/10.1038/cddis.2016.321.

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Brooks, David, Fawwaz Naeem, Marta Stetsiv, Samantha C. Goetting, Simranjot Bawa, Nicole Green, Cheryl Clark, Arash Bashirullah, and Erika R. Geisbrecht. "Drosophila NUAK functions with Starvin/BAG3 in autophagic protein turnover." PLOS Genetics 16, no. 4 (April 22, 2020): e1008700. http://dx.doi.org/10.1371/journal.pgen.1008700.

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Franco, Renato, Giosuè Scognamiglio, Vincenzo Salerno, Adolfo Sebastiani, Giovanni Cennamo, Paolo A. Ascierto, Gerardo Botti, Maria C. Turco, and Alessandra Rosati. "Expression of the Anti-Apoptotic Protein BAG3 in Human Melanomas." Journal of Investigative Dermatology 132, no. 1 (January 2012): 252–54. http://dx.doi.org/10.1038/jid.2011.257.

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Bruno, Anna Paola, Francesca Isabella De Simone, Vittoria Iorio, Margot De Marco, Kamel Khalili, Ilker Kudret Sariyer, Mario Capunzo, Stefania Lucia Nori, and Alessandra Rosati. "HIV-1 Tat protein induces glial cell autophagy through enhancement of BAG3 protein levels." Cell Cycle 13, no. 23 (October 29, 2014): 3640–44. http://dx.doi.org/10.4161/15384101.2014.952959.

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Zhang, Jiankai, Zhangyou He, Wenjian Xiao, Qingqing Na, Tianxiu Wu, Kaixin Su, and Xiaojun Cui. "Overexpression of BAG3 Attenuates Hypoxia-Induced Cardiomyocyte Apoptosis by Inducing Autophagy." Cellular Physiology and Biochemistry 39, no. 2 (2016): 491–500. http://dx.doi.org/10.1159/000445641.

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Background: Hypoxia is a well-known factor in the promotion of apoptosis, which contributes to the development of numerous cardiac diseases, such as heart failure and myocardial infarction. Inhibiting apoptosis is an important therapeutic strategy for the treatment of related heart diseases caused by ischemia/hypoxic injury. Previous studies have demonstrated that BAG3 plays an important role in cardiomyocyte apoptosis and survival. However, the role of BAG3 in hypoxia-induced cardiomyocyte apoptosis remains to be clarified. Here, we demonstrate that BAG3 is induced by hypoxia stimuli in cultured cardiomyocytes. Methods: BAG3 expression level was measured in H9c2 cells treated with hypoxia for 48 h. Cell proliferation and apoptosis were tested using MTT assay and Annexin V FITC-PI staining assay, respectively. The mRNA or protein expression level of BAG3, LC3-I, LC3-II, Atg5, NF-κB p65 and phosphorylated NF-κB p65 were assessed by qRT-PCR and western blot assay, respectively. Resluts: Overexpression of BAG3 inhibited cell apoptosis and promoted proliferation in hypoxia-injured H9c2 cells. Furthermore, autophagy and NF-κB were activated by BAG3 overexpression, and the NF-κB inhibitor PDTC could inhibit the activation of autophagy induced by BAG3 overexpression. In addition, the autophagy inhibitor 3-MA partly impeded the inhibitory effect of BAG3 on hypoxia-induced cardiomyocyte apoptosis. Conclusion: these results suggested that overexpression of BAG3 promoted cell proliferation and inhibited apoptosis by activating autophagy though the NF-κB signaling pathway in hypoxia-injured cardiomyocytes.

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Romano, Maria Fiammetta, Michelina Festa, Antonello Petrella, Maria Pascale, Rita Bisogni, Vincenzo Poggi, Elise C. Kohn, Salvatore Venuta, Maria Caterina Turco, and Arturo Leone. "BAG3 Protein Regulates Cell Survival in Childhood Acute Lymphoblastic Leukemia Cells." Cancer Biology & Therapy 2, no. 5 (May 4, 2003): 508–10. http://dx.doi.org/10.4161/cbt.2.5.524.

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Basile, Anna, Morena d'Avenia, Alessandra Rosati, Michelina Festa, Antonia Falco, Maria Turco, and Maria Pascale. "Novel Targets for Apoptosis Modulation: BAG3 Protein and Other Co- Chaperones." Recent Patents on Endocrine, Metabolic & Immune Drug Discovery 3, no. 2 (June 1, 2009): 80–86. http://dx.doi.org/10.2174/187221409788452318.

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Bonelli, P., A. Petrella, A. Rosati, M. F. Romano, R. Lerose, M. G. Pagliuca, T. Amelio, et al. "BAG3 protein regulates stress-induced apoptosis in normal and neoplastic leukocytes." Leukemia 18, no. 2 (November 20, 2003): 358–60. http://dx.doi.org/10.1038/sj.leu.2403219.

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Cesaro, E., G. Montano, A. Rosati, R. Crescitelli, P. Izzo, M. C. Turco, and P. Costanzo. "WT1 protein is a transcriptional activator of the antiapoptotic bag3 gene." Leukemia 24, no. 6 (April 22, 2010): 1204–6. http://dx.doi.org/10.1038/leu.2010.68.

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De Marco, Margot, Maria Caterina Turco, and Alessandra Rosati. "BAG3 protein is induced during cardiomyoblast differentiation and modulates myogenin expression." Cell Cycle 10, no. 5 (March 2011): 850–52. http://dx.doi.org/10.4161/cc.10.5.14964.

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Shemetov, Anton A., and Nikolai B. Gusev. "Biochemical characterization of small heat shock protein HspB8 (Hsp22)–Bag3 interaction." Archives of Biochemistry and Biophysics 513, no. 1 (September 2011): 1–9. http://dx.doi.org/10.1016/j.abb.2011.06.014.

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Zhou, Jiechao, Hei-Man Chow, Yan Liu, Di Wu, Meng Shi, Jieyin Li, Lei Wen, et al. "Cyclin-Dependent Kinase 5–Dependent BAG3 Degradation Modulates Synaptic Protein Turnover." Biological Psychiatry 87, no. 8 (April 2020): 756–69. http://dx.doi.org/10.1016/j.biopsych.2019.11.013.

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Ijabi, Roghayeh, Parisa Roozehdar, Reza Afrisham, Hemen Moradi-Sardareh, Saeed Kaviani, Janat Ijabi, and Amirhossein Sahebkar. "Association of GRP78, HIF-1α and BAG3 Expression with the Severity of Chronic Lymphocytic Leukemia." Anti-Cancer Agents in Medicinal Chemistry 20, no. 4 (May 15, 2020): 429–36. http://dx.doi.org/10.2174/1871520619666191211101357.

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Introduction: Parallel with the progression of Chronic Lymphocytic Leukemia (CLL), the levels of 78KDa Glucose-Regulated Protein (GRP78) and Hypoxia-Inducible Factor 1 alpha (HIF-1α) are increased as they may activate the induction of anti-apoptotic proteins such as BCL2 Associated Athanogene 3 (BAG3). Previous studies have indicated that there is a positive correlation among GRP78, HIF-1α and BAG3. Objective: This study aimed to evaluate the effect of metabolic factors involved in invasive CLL on apoptotic factors. Methods: A case-control study was conducted on 77 patients diagnosed with CLL along with 100 healthy individuals. Cell blood count was performed for all participants. According to Binet's classification, CLL patients were divided into different groups. B cells were isolated from the peripheral blood of CLL patients by binding to anti-CD19 beads. The expression of BAG3, GRP78 and HIF-1α genes was analyzed using the RT-PCR method. To confirm the results of RT-PCR, western blot analysis was carried out. Results: The results showed that there was a strong association among the expression of BAG3, GRP78 and HIF-1α. The stage of CLL in patients was highly correlated with the expression rate of each gene (p<0.001). Accordingly, the western blot analysis indicated that the concentrations of GRP78 and HIF-1α were significantly higher than the expression of BAG3, considering the stage of CLL. Conclusion: It was shown that increased expression of GRP78 and HIF-1α could result in the elevation of BAG3, as well as the disease progression. Therefore, the role of these metabolic factors might be more pronounced compared with the anti-apoptotic agents to monitor disease progression in CLL patients.

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Li, Xiaokai, Teresa Colvin, Jennifer N. Rauch, Diego Acosta-Alvear, Martin Kampmann, Bryan Dunyak, Byron Hann, et al. "Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer." Molecular Cancer Therapeutics 14, no. 3 (January 6, 2015): 642–48. http://dx.doi.org/10.1158/1535-7163.mct-14-0650.

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Zhang, Liang, Zhi-Ping Zhang, Xian-En Zhang, Fu-Sen Lin, and Feng Ge. "Quantitative Proteomics Analysis Reveals BAG3 as a Potential Target To Suppress Severe Acute Respiratory Syndrome Coronavirus Replication." Journal of Virology 84, no. 12 (April 14, 2010): 6050–59. http://dx.doi.org/10.1128/jvi.00213-10.

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ABSTRACT The discovery of a novel coronavirus (CoV) as the causative agent of severe acute respiratory syndrome (SARS) has highlighted the need for a better understanding of CoV replication. The replication of SARS-CoV is highly dependent on host cell factors. However, relatively little is known about the cellular proteome changes that occur during SARS-CoV replication. Recently, we developed a cell line expressing a SARS-CoV subgenomic replicon and used it to screen inhibitors of SARS-CoV replication. To identify host proteins important for SARS-CoV RNA replication, the protein profiles of the SARS-CoV replicon cells and parental BHK21 cells were compared using a quantitative proteomic strategy termed “stable-isotope labeling by amino acids in cell culture-mass spectrometry” (SILAC-MS). Our results revealed that, among the 1,081 host proteins quantified in both forward and reverse SILAC measurements, 74 had significantly altered levels of expression. Of these, significantly upregulated BCL2-associated athanogene 3 (BAG3) was selected for further functional studies. BAG3 is involved in a wide variety of cellular processes, including cell survival, cellular stress response, proliferation, migration, and apoptosis. Our results show that inhibition of BAG3 expression by RNA interference led to significant suppression of SARS-CoV replication, suggesting the possibility that upregulation of BAG3 may be part of the machinery that SARS-CoV relies on for replication. By correlating the proteomic data with these functional studies, the findings of this study provide important information for understanding SARS-CoV replication.

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Lövenich, Lukas, Georg Dreissen, Christina Hoffmann, Jens Konrad, Ronald Springer, Jörg Höhfeld, Rudolf Merkel, and Bernd Hoffmann. "Strain-induced mechanoresponse depends on cell contractility and BAG3-mediated autophagy." Molecular Biology of the Cell 32, no. 20 (October 1, 2021): ar9. http://dx.doi.org/10.1091/mbc.e21-05-0254.

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The mechanosensitivity of mammalian cells and protein degradation via autophagy are two essential regulatory cell mechanisms. The close interplay between these two mechanisms is characterized in detail and proves a strong bidirectional cross-talk between BAG3-mediated chaperone-assisted selective autophagy and mechanosensitivity.

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Rauch, Jennifer N., Eric Tse, Rebecca Freilich, Sue-Ann Mok, Leah N. Makley, Daniel R. Southworth, and Jason E. Gestwicki. "BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins." Journal of Molecular Biology 429, no. 1 (January 2017): 128–41. http://dx.doi.org/10.1016/j.jmb.2016.11.013.

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Guerriero, L., K. Chong, R. Franco, A. Rosati, F. De Caro, M. Capunzo, M. C. Turco, and D. SB Hoon. "BAG3 protein expression in melanoma metastatic lymph nodes correlates with patients’ survival." Cell Death & Disease 5, no. 4 (April 2014): e1173-e1173. http://dx.doi.org/10.1038/cddis.2014.143.

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