ProteostaSys: a systems view of proteostasis

08 - 09 September 2025 08:45 - 17:00 Hilton Cambridge City Centre Free
Request an invitation

Theo Murphy meeting organised by Dr Ritwick Sawarkar, Professor Rick Morimoto, Professor Lea Sistonen, and Dr Anat Ben-Zvi.

Proteostasis underpins the homeostasis of the functional proteome and is implicated in most age-related disease conditions. The proposed meeting will capitalise on the recent definition of the human proteostasis network to bring together experts from molecular cell biology and quantitative systems biology. The meeting will facilitate interdisciplinary discussions and proteostasis to speed up fundamental discoveries with biomedical implications.

Programme

The programme, including the speaker biographies and abstracts, will be available soon. Please note the programme may be subject to change.

Poster session

There will be a poster session on Monday 08 September. If you would like to present a poster, please submit your proposed title, abstract (up to 200 words), author list, and the name of the proposed presenter and institution to the Scientific Programmes team. Acceptances may be made on a rolling basis so we recommend submitting as soon as possible in case the session becomes full. Submissions made within one month of the meeting may not be included in the programme booklet.

Attending this event

  • Free to attend and in-person only
  • When requesting an invitation, please briefly state your expertise and reasons for attending
  • Requests are reviewed by the meeting organisers on a rolling basis. You will receive a link to register if your request has been successful
  • Catering options will be available to purchase upon registering. Participants are responsible for booking their own accommodation. Please do not book accommodation until you have been invited to attend the meeting by the meeting organisers

Enquiries: contact the Scientific Programmes team.

Organisers

  • Dr Ritwick Sawarkar, University of Cambridge, UK

    Dr Ritwick Sawarkar, University of Cambridge, UK

    Ritwick studied Microbiology and Biochemistry in Mumbai (India) and obtained his PhD in 2010 from the Indian Institute of Science, Bangalore (India). Ritwick then moved to the Department of Biosystems Science and Engineering of ETH-Zürich in Basel (Switzerland) as a postdoctoral fellow. In 2014, Ritwick started his own independent group at the Max Planck Institute of Immunobiology and Epigenetics in Freiburg (Germany), before moving to the University of Cambridge (UK) in 2019.

  • Professor Richard Morimoto

    Professor Richard Morimoto

    Dr Richard I Morimoto is the Bill and Gayle Cook Professor of Biology and Director of the Rice Institute for Biomedical Research at Northwestern University. Rick received his BS from the University of Illinois at Chicago, subsequently received a PhD in Molecular Biology at the laboratory of Professor Murray Rabinowitz, University of Chicago in 1978. He then conducted his postdoctoral research in the laboratory of Professor Matthew Meselson in the Department of Biochemistry and Molecular Biology at Harvard University in Cambridge, MA. He was concurrently a Tutor in Biochemical Sciences at Harvard College. In 1982, Morimoto joined the faculty of the Department of Biochemistry, Molecular Biology, and Cell Biology at Northwestern University in Evanston, IL. He has served as the Chair of Biochemistry, Molecular Biology, and Cell Biology, the Dean of The Graduate School, and the Associate Provost of Graduate Education at Northwestern. He has given talks at universities and symposia throughout the world and has been a Visiting Professor at Åbo Akademi University in Finland, Beijing University, École Normale Supérieure in Paris, Kyoto University, Kyoto Sangyo University, Osaka University, University of Rome, Technion University in Israel and the University of Cambridge. He was a founder of the biotech company Proteostasis Therapeutics, Inc in Cambridge MA, to develop small molecule therapeutics to treat diseases of protein homeostasis.

  • Professor Lea Sistonen

    Professor Lea Sistonen

    Lea Sistonen is Professor of Cell and Molecular Biology at Åbo Akademi University (Turku, Finland) since 2000 and Group Leader at Turku Bioscience Center (University of Turku and Åbo Akademi University) since 1994. In 1990, she obtained the PhD degree in Molecular Genetics, specifically Cancer Biology, from the University of Helsinki, Finland. After a 3.5-year post-doctoral training on the molecular basis of cellular stress responses in the laboratory of Richard I Morimoto at Northwestern University, Evanston, IL, US, she returned to Finland and started as a PI. Her expertise is in the field of the transcriptional regulation of cellular stress responses and how the same molecular factors, e.g. heat shock factors (HSFs) regulate also normal physiological processes, such as gametogenesis, and how they are deregulated in human diseases, such as cancer. Her studies on genome-wide transcriptional programs have contributed to our understanding of the maintenance of protein homeostasis (proteostasis), not only in acute stress but also during normal growth and development as well as in malignant transformation. Using ChIP-seq and PRO-seq techniques in human cells, the Sistonen laboratory has demonstrated the functional relationship between the occupancy of HSFs, changes in the chromatin architecture and de novo transcription of both genes and enhancers.

  • Professor Anat Ben-Zvi

    Professor Anat Ben-Zvi

    Professor Anat Ben-Zvi is an associate professor at the Ben-Gurion University of the Negev, Department of Life Science. Professor Ben-Zvi has received her PhD degree in Biochemistry from the Hebrew University of Jerusalem, where she worked under the supervision of Professor Pierre Goloubinoff. Working at the Hebrew University of Jerusalem and the University of Lausanne on molecular chaperones and developing a new model for the HSP70 chaperone functional mechanism and its role in protein disaggregation. She then moved to Northwestern University at Evanston, USA, and joined the group of Professor Richard Morimoto as a post-doctoral affiliate. She focused on the regulation of cellular protein homeostasis (proteostasis). Together with other group members of the Morimoto group, they established C. elegans as a model organism to study protein folding and misfolding in a multicellular organism and went on to demonstrate the impact of protein misfolding and aging on organismal proteostasis. Professor Ben-Zvi established her own research group at the Ben-Gurion University of the Negev in 2010. Her group studies the dynamics of quality control networks during the lifespan of an organism. Specifically, her group aims to understand how proteostasis in a multicellular organism is regulated during development and why it fails in aging and disease.

Schedule

Chair

Professor Laura Itzhaki

Dr Laura Itzhaki

University of Cambridge, UK

08:45-09:00 Welcome by the lead organisers
09:00-09:20 Regulation of the Huntington folding landscape by Hsc70, DNAJB1 and Apg2

Molecular chaperones play crucial roles in protein folding, targeting, sequestration, disaggregation, and degradation of misfolded proteins. Their intervention is critical in preventing the conversion of proteins from their native states into amyloid fibrils. Key components in this chaperone network are the HSPA complexes, particularly involving J-domain proteins (JDPs), which drive the HSPA folding machinery by delivering substrates and activating the HSPA ATPase. A focus of Janine Kirstein’s research is the analysis of the versatility of the incredibly diverse JDP family with 50 different JDPs identified in humans. A well-studied JDP-HSPA chaperone complex, comprising DNAJB1, Hsc70, and the NEF Apg2, can suppress Huntingtin Exon1Q48 (HTT) aggregation in an ATP-dependent manner. DNAJB1 binds with a specific motif located between CTDI and CTDII to the polyQ-adjacent proline rich domain of HTT. Mutation of the highly conserved H244 of the motif in DNAJB1 completely abrogates the suppression of HTT aggregation and disaggregation of HTT fibrils by the trimeric chaperone complex. Notably, this mutation does not affect the binding and remodelling of any other tested protein substrate including amyloid proteins, suggesting that the generalist DNAJB1 uses unique site for the interaction with distinct protein substrates such as HTT. Surprisingly, while an overexpression of DNAJB1 is protective in HTT expressing cultured cells, it is detrimental on an organismal level. Overexpression of the DNAJB1 homolog, DNJ-13 leads to an increase in HTT aggregation, spreading and toxicity in C. elegans. Increased levels of DNJ-13 might boost the disaggregation activity of the trimeric chaperone complex in vivo and thereby generate seeding-competent HTT species that favour aggregation and spreading of HTT.

Professor Janine Kirstein

Professor Janine Kirstein

Leibniz Institute on Aging, Germany

11:00-11:20 CBFA2T2 regulates lipid metabolism in complex with the transcription factor HSF1 and histone demethylase KDM3C

The heat shock response (HSR) is an evolutionarily conserved mechanism to maintain proteostasis and is characterised by induction of heat shock proteins (HSPs) in proteotoxic stress conditions. This induction is regulated mainly at transcriptional level by heat shock transcription factors (HSFs). HSF1 is a master regulator of the HSR in human cells and regulate the expression of not only HSP genes but also a variety of genes involved in cell proliferation and metabolism under conditions without environmental stresses. HSF1 could access to and activate these target genes probably by recruiting histone-modifying enzymes and chromatin-remodelling complexes. However, HSF1-mediated regulatory mechanisms of metabolism-related genes are not well known. Here, we identified a transcriptional co-regulator CBFA2T2 as an HSF1-interacting protein irrespective of heat shock. CBFA2T2 and HSF1 up-regulate a common set of genes involved in lipid metabolism, including SREBP1, SREBP2 and SOAT1, in melanoma MeWo cells. Remarkably, HSF1 binding to the promoters of these genes required CBFA2T2, whereas CBFA2T2 occupied them even in the absence of HSF1. CBFA2T2 accesses to the target gens through the recruitment of PBAF chromatin remodelling complex and transcription factors such as PRDM1. CBFA2T2 and HSF1 co-operate to recruit the histone demethylase KDM3C, which regulates lipid metabolism. Blockage of the interaction between CBFA2T2 and HSF1 inhibited lipid droplet formation and proliferation of melanoma cells. Our observations provide regulatory mechanisms of HSF1-mediated expression of lipid metabolism-related genes, which support melanoma tumorigenesis.

Professor Akira Nakai

Professor Akira Nakai

Yamaguchi University, Japan

11:20-11:40 Regulation of protein homeostasis in oocyte aging

Female reproductive aging starts in humans at the average age of 35, when a significant number of oocytes are still present while oocyte quality rapidly declines. During postnatal oogenesis, the primary oocytes arrested at meiotic prophase I undergo robust protein synthesis in the growth phase to prepare the machinery for meiotic maturation and maternal factors for subsequent embryogenesis, making oogenesis particularly reliant on proteostasis. Data from Dr Li and colleagues suggest proteostasis decline is a driving force of oocyte aging. In both C. elegans and mice, loss of HSF1 activities is an early event of oocyte aging, leading to reduced expression of chaperone genes and insufficient protein folding capacity. Depletion of HSF-1 from C. elegans oocytes phenocopies the maladaptive stress responses observed in maternal aging, which ultimately undermines oocyte proteostasis and quality. Conversely, over-expression of HSF-1 in the germline preserves oocyte quality and reduces chromosomal errors in maternal aging. Remarkably, Dr Li and colleagues found that three well-established pro-reproductive longevity signaling pathways in C. elegans (insulin/IGF-1, TGF-b-Sma/Mab, and mTORC2-SGK-1) converge on the regulation of protein synthesis in germ cells to suppress the reproductive defects associated with HSF-1 depletion and preserve oocyte proteostasis in maternal aging.

Dr Jian Li

Dr Jian Li

New York Medical College, USA

11:40-12:00 Age-dependent fluctuations in the Hsp90 interaction network

Molecular chaperones are sentinels of the protein homeostasis (proteostasis) process and are required to safeguard polypeptides by continuously scrutinising the conformational status of all cellular proteins. Insights into proteostasis primarily have been gained by studying protein biogenesis and triage events. Yet, the proverbial birth and death of any polypeptide only represents a small percentage of the protein-lifecycle. The mainstay of a protein’s time is spent functioning in pathways to support life. While it has long been suggested that molecular chaperones regulate native proteins, how any chaperone might recognise and/or modulate the broad spectrum of mature proteins found within a cell had been poorly understood. Recently, we developed a high-throughput chemical biology tactic to discover that the Hsp90 chaperone targets intrinsically disordered regions (IDRs) of native proteins to broadly interact with a cell’s protein population (eg, yeast Hsp90 associates with ~25% of the proteome). We have exploited this system to investigate how the Hsp90 interaction landscape shifts during the aging process. Our presented work will show that low Hsp90 protein levels are insufficient to support normal aging, cells with reduced Hsp90 have elevated protein aggregates at early timepoints during chronological aging, and the physical interaction network surrounding Hsp90 shifts as cells age including a rewiring of the chaperone system. Overall, our data demonstrate that Hsp90 acts as a key aging factor by functioning as a central hub in the proteostasis process.

Professor Brian Freeman

Professor Brian Freeman

University of Illinois, USA

Chair

Professor Stefan Marciniak

Stefan Marciniak

University of Cambridge, UK

13:30-13:50 Unveiling non-cell autonomous mechanisms in alpha-synuclein pathobiology: insights from C. elegans

Pathological alpha-synuclein condensation and toxicity are associated with a range of age-related neurodegenerative diseases, including Parkinson’s disease and multiple system atrophy (MSA). However, the biological triggers and consequences of these pathological changes are not completely understood. Previous screens in a C. elegans model, capturing both condensation- and toxicity features of alpha-synuclein, have revealed several biological interventions that counter alpha-synuclein pathology. These interventions include metabolic rewiring, such as the inhibition of organismal tryptophan degradation, and microbiome replacement. However, the protective mechanisms underlying these interventions remain unclear. This presentation highlights ongoing research aimed at identifying the mechanisms of such non-cell-autonomous protection. Using diverse biological screens in both C. elegans and protective microbiota, previously unknown regulators and microbial metabolites were identified that modify alpha-synuclein pathobiology. These results provide insight into the impact of systemic factors and host-microbiome interactions in the development of synucleinopathies.

Professor Ellen Nollen

Professor Ellen Nollen

University Medical Center Groningen, The Netherlands

13:50-14:10 Alpha-synuclein and tau aggregates polymorphism and the structural molecular basis of diverse synucleinopathies and tauopathies

The aggregation of the proteins alpha-synuclein (a-Syn) and tau within the central nervous system is deleterious and associated to diverse neurodegenerative disorders. How a-Syn and tau aggregates target defined cells, how those aggregates traffic between them, multiply by recruiting their endogenous counterparts and cause distinct synucleinopathies and tauopathies is still poorly understood.

Proteostasis decline favors a-Syn and tau aggregation. Evidences for a-Syn and tau aggregates-mediated sequestration of important proteins, among which molecular chaperones and members of the cellular clearance machinery that mimick their loss of function, will be presented and discussed. A-Syn and tau aggregates are also released from affected neuronal cells after multiplication, they bind to naïve neurons cell membranes and redistribute protein receptors with functional consequences that will be detailed.

The reason why the aggregation of a-Syn causes distinct synucleinopathies was unknown until we showed this protein to form structurally different fibrillar aggregates in test tubes and proposed that the different structures may cause different pathologies. How the diversity of a-Syn and tau fibrillar aggregates, including those derived from patient brains, cause distinct diseases will be discussed.

The importance of targeting the surfaces of aggregated a-Syn and tau from the diagnostic and therapeutic standpoints will be highlighted and discussed.

Dr Ronald Melki

Dr Ronald Melki

Centre national de la recherche Scientifique, France

09:00-09:20 Neuronal regulation of cellular stress responses in metazoans: mechanisms and open questions

Tremendous advances have been made in understanding how isolated cells autonomously respond to stress. However, it remains unclear whether the same principles apply within the complex environments of tissues and organ systems in metazoans. Building on our discovery that the heat shock response—one of the most ancient and conserved stress response pathways—is not solely cell-autonomous in the nematode Caenorhabditis elegans, but instead regulated by sensory neuronal circuits, our research aims to elucidate how neuronal stress sensing modulates protective responses in distant target cells. We will discuss our progress in uncovering the fundamental mechanisms by which the nervous system of multicellular organisms translates the sensory detection of stress into anticipatory, cell-type-specific transcriptional programs—activated before damage occurs and tailored to the nature of the stressor. We will also speculate on how discoveries in this field could redefine our understanding of stress response regulation in vivo and reveal how systemic coordination enhances organismal resilience.

Professor Veena Prahlad

Professor Veena Prahlad

Roswell Park Cancer Institute, USA

09:20-09:40 An unexpected partnership: understanding how HSF-1 and mitochondria cooperate to promote healthy ageing

The transcription factor HSF-1 has long been recognised as the master regulator of the Heat Shock Response (HSR), a highly conserved transcriptional programme that is rapidly deployed to counter the threat of misfolded proteins within the cytosol/nucleus. In keeping with this role, impaired HSF-1 activity is associated with reduced tissue resilience, shortened lifespan and increased susceptibility to age-associated protein conformational disease, while enhanced HSF-1 activity is associated with greater stress resistance, increased lifespan and improved protection against protein aggregation and proteotoxicity. While HSF-1 is classically thought to promote tissue-health by increasing the levels of cytosolic/nuclear molecular chaperones and protein degradation factors, evidence is emerging that HSF-1 activity is also closely coupled to mitochondrial homeostasis. In this talk, I will present my groups recent findings that increased HSF-1 activity converges on mitochondrial homeostasis through the proteasome shuttling factor, ubiquilin-1. HSF-1 promotes ubiquilin-1 expression, which leads to increased turnover of the CDC-48 co-factor, NPL-4. This alters mitochondrial network dynamics and leads to metabolic changes that promote longevity. In addition, changes in mitochondrial homeostasis result in increased HSF-1 activity and protection of the cytosolic proteome. Our findings reveal that HSF-1 sits at the nexus between cytosolic and mitochondrial homeostasis and suggest that the interplay between HSF-1 and mitochondria is a key determinant of cell and tissue viability that could be manipulated to promote healthy ageing.

Dr John Labbadia

Dr John Labbadia

University College London, UK

09:40-10:00 Regulation of stress granule dynamics by the Hsp70 chaperone system

Stress granules (SGs) are ribonucleoprotein condensates that transiently form during cellular stress when protein translation is inhibited. They allow the storage of RNA-binding proteins and mRNAs, and their release for translation restoration upon stress recovery. Loss of SG dynamic properties is proposed to underlie the formation of protein aggregates in certain neurodegenerative diseases, including amyotrophic lateral sclerosis. The Hsp70 chaperone family has been implicated in limiting aberrant SG aggregation and in the disassembly of the condensates during recovery. However, a detailed understanding of how Hsp70 regulates SG dynamic properties is lacking. Here, we used C. elegans to investigate the role of constitutively expressed Hsp70 (HSP-1/Hsc70) in the dynamics of SGs in different cell types. We found that HSP-1 associates with cytosolic structures corresponding to bona fide SGs throughout the tissues of the animal. Fluorescence recovery after photobleaching of SGs in various cell types revealed that HSP-1 is highly mobile and rapidly exchanges with the cytoplasmic pool, in contrast to the core SG protein GTBP-1/G3BP1, but similar to other SG components. Reduced hsp-1 function resulted in persistent SGs in germ cells, indicating a role in SG disassembly, and altered the mobility of select SG components, suggesting a stronger effect on the more dynamic shell within the SG structure. These findings provide insights into the regulation of condensate dynamics and architecture by Hsp70, with potential implications for pathological transitions of SGs.

Dr Ambre Sala

Dr Ambre Sala

Institute for Integrative Biology of the Cell, France

11:40-12:00 Impaired sphingolipid homeostasis exacerbates tau pathology by disrupting endolysosomal integrity through endomembrane rigidification

The progression of neurodegenerative diseases such as Alzheimer’s disease (AD) or Parkinson’s disease (PD), is linked to the spreading of protein aggregation across interconnected brain regions. Fibrillar seeds are transferred between cells, inducing misfolding and aggregation of its native monomeric counterpart. A critical rate-limiting step in this process is the rupture of endolysosomal vesicles, which releases transferred aggregates into the cytosol, where they promote further aggregation of endogenous proteins. While the pathways underlying endolysosomal damage and repair have been increasingly studied, many aspects remain unclear. We conducted a genome-wide RNAi screen in a novel C. elegans model of tau spreading and identified sphingolipid metabolism genes as critical for endolysosomal integrity. Using C. elegans and cell culture models, we investigated how disruption of sphingolipid homeostasis affects endolysosomal membrane integrity and contributes to tau aggregation and toxicity. Fluorescence recovery after photobleaching and C-Laurdan dye imaging revealed that silencing sphingolipid metabolism genes decreases endolysosomal vesicle membrane fluidity, increasing endolysosomal rupture. The accumulation of aggregated tau in endolysosomal vesicles further aggravated endomembrane rigidification and damage and promoted seeded tau aggregation, potentially by facilitating the escape of tau seeds from the endolysosomal system. Supplementation with unsaturated fatty acids improved membrane fluidity, suppressing endolysosomal rupture and seeded tau aggregation in cell models, and alleviating tau-associated neurotoxicity in C. elegans. Conversely, supplementation with the saturated fatty acid palmitic acid worsened these effects. These findings provide insights into how impaired sphingolipid homeostasis drives tau pathology, suggesting membrane fluidity restoration as a potential therapeutic strategy for AD.

Professor Carmen Nussbaum

Professor Carmen Nussbaum

Ludwig Maximilians University Munich, Germany

Chair

Dr Rahul Samant

Dr Rahul Samant

Babraham Institute, UK

13:30-13:50 Exposure to microplastic disrupts proteostasis in Caenorhabditis elegans

Since the 1950s, humans have produced 8 billion tons of plastic. This plastic, the vast majority of which is not recycled, is in the form of plastic containers, synthetic fibers used in clothing, paints, adhesives, etc. These plastics break down with use and enter our food and water as micro and nano-sized particles. Plastic is also added to personal care products as microspheres that do not need to break down to enter waterways. Moreover, tire wear particles account for 28% of microplastics that enter the environment. A recent retrospective study revealed that microplastic accumulation in the human brain is increasing at an alarming rate. This has been found to contribute to neuroinflammation and to promote the progression of Alzheimer’s Disease symptoms. We asked whether microplastic from a synthetic soccer turf (micro-rubber) causes protein damage/misfolding, overwhelms the proteostasis network, and contributes to proteostasis collapse. To address this, we utilised C. elegans sensors of protein folding, and found that exposure to micro-rubber particles accelerated the formation of large visible protein aggregates in body wall muscle cells. Interestingly, animals that were exposed to micro-rubber were impaired in their ability to launch a heat shock response. Taken together, the data suggests that micro-rubber particles contribute to a decline in proteostasis, which may be relevant to neurodegenerative disease progression.

Dr Elise A Kikis

Dr Elise A Kikis

University of the South (Sewanee), UK

13:50-14:10 Intersections between protein oxidation-reduction pathways and proteostasis at the subcellular level 

Protein disulfide formation contributes to protein folding and function, as evidenced by numerous oxidoreductases that maintain disulfide status within various cell compartments.  Many of these oxidoreductases, including thioredoxins (Trxs) and protein disulfide isomerases (PDIs), arose from a common evolutionary precursor and employ transient thiol-disulfide exchange mechanisms when interacting with their redox partners.  Because disulfide bonds that form between Trx superfamily members and their redox partners are often short-lived, we developed a chemical cross-linking strategy that irreversibly captures these proteins when interacting with potential redox partners.  Using the thiol-reactive cross-linker divinyl sulfone (DVSF), Trx2, a cytosolic Trx in baker’s yeast, undergoes cross-linking with its most prominent redox partners via modification of its active site cysteines. Likewise, upon DVSF treatment, PDIs that promote oxidative protein folding in the ER form cross-linked complexes with known redox partners, including many chaperones and protein clearance factors. More recently, we have turned our attention to less studied redox networks, seeking to identify the interaction partners of disulfide maintenance systems in mitochondria.  Particularly, we have characterised the putative redox partners of yeast Trx3, a disulfide reductase that resides in the mitochondrial matrix. We have found that Trx3 interacts with numerous metabolic enzymes, including members of the branched chain amino acid biosynthesis pathway, as well as proteins in the proteostasis network.  Our current work suggests disulfide bond homeostasis and flux through specific metabolic pathways may be linked in previously undescribed ways.

Professor James West

Professor James West

The College of Wooster, USA

14:10-14:30 Microbial pathogenesis in neurodegenerative protein conformational diseases

There is no cure or effective treatment for neurodegenerative protein conformational diseases (PCDs), such as Alzheimer’s, Parkinson’s, and Huntington’s. All these ailments are characterised by toxic protein aggregation, resulting in progressive neuronal damage and cell death. Emerging evidence reveals that bacteria play a significant role in the pathogenesis of neurodegenerative diseases; however, the microbial identity and the underlying mechanisms remain elusive. In a screen of over 220 unique bacterial species from the Human Microbiome Project, we found proteotoxic and proteoprotective bacteria. We demonstrated that employing bacteriophage-mediated strategies to eliminate detrimental bacteria associated with proteotoxicity alleviates disease pathogenicity. Furthermore, among the beneficial microbes, a single bacterial strain, Prevotella corporis, provides protection against misfolding and aggregation. We employed the Caenorhabditis elegans and Drosophila melanogaster models expressing polyglutamine and Aβ42 to demonstrate that colonisation of the gut suppresses aggregation in both models. Further analysis revealed that P. corporis activates the expression of heat shock genes and can rapidly disassemble existing protein aggregates. While P. corporis did not have any effect on lifespan, it enhanced the thermotolerance and disaggregation activity of the host, suggesting general improvement in proteostasis. Collectively, we reveal how bacteria affect host proteostasis and influence disease pathology, opening new opportunities to manage neurodegenerative diseases by targeting the gut.

Dr Daniel Czyż

Dr Daniel Czyż

University of Florida, USA