Chiosis Lab

Dive deeper into our @cp-trendsbiochem.bsky.social cover article! Read more on @springernature.com Communities:
communities.springernature.com/posts/when-m...
#Epichaperome #PTMs #NetworkBiology #SystemsBiology #TrendsBiochem #NatureCommunities

📸Check out a few photos from @gabrielachiosis.bsky.social and Tanaya's talks at #CSSI2025 @stresscell.bsky.social l last weekend.
#epichaperome #cellularstress #HSP90 #Alzheimers

📢 Our October issue is now online. Access the full issue 👉 www.cell.com/trends/bioch....

🎨 The cover highlights a Review from @chiosislabmskcc.bsky.social‬ and co on how PTMs reprogram chaperones into epichaperomes.

PTMs as molecular encoders: reprogramming chaperones into epichaperomes for network control in disease Recent discoveries reveal that post-translational modifications (PTMs) do more than regulate protein activity – they encode conformational states that…

💡Have you checked out our latest review in @cp-trendsbiochem.bsky.social? Discover how post-translational modifications can convert molecular chaperones into #epichaperomes – stable scaffolds that restructure protein–protein interaction networks in disease #PPI
www.sciencedirect.com/science/arti...

Out now in @cp-trendsbiochem.bsky.social: "PTMs as Molecular Encoders: Reprogramming Chaperones into Epichaperomes for Network Control in Disease" from @chiosislabmskcc.bsky.social. Learn more ⬇️

🌟Very excited to share that our article 'PTMs as Molecular Encoders: Reprogramming Chaperones into Epichaperomes for Network Control in Disease' is out online now in @cp-trendsbiochem.bsky.social
#PTMs #HSP90 #epichaperome #PPI #neuroscience @mskcancercenter.bsky.social
doi.org/10.1016/j.ti...

📝 Online now - the Review "PTMs as molecular encoders: reprogramming chaperones into epichaperomes for network control in disease" from @chiosislabmskcc.bsky.social et al.

#ProteinProteinInteractions #ProteinNetworks #ChaperoneReprogramming

Read it here 👉 authors.elsevier.com/sd/article/S...

Sahil presented earlier this month at #AAIC2025 in Toronto @alzassociation.bsky.social
This work was supported by BrightFocus & NIH Aging and aims to advance #precisionmedicine in #neurodegeneration through the development of small molecule probes for #epichaperome imaging in #Alzheimers.

Introducing dysfunctional Protein-Protein Interactome (dfPPI) – A platform for systems-level protein-protein interaction (PPI) dysfunction investigation in disease Protein-protein interactions (PPIs) play a crucial role in cellular function and disease manifestation, with dysfunctions in PPI networks providing a …

🧵Have you checked out our recent article in
Current Opinion in Structural Biology? Follow this thread by Chiosis Lab postdoc Souparna Chakrabarty
to learn about the Dysfunctional Protein-Protein Interactome (#dfPPI) - a #chemoproteomic platform www.sciencedirect.com/science/arti... 🧵(1/11)

Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation - Nature Communications Epichaperomes are chaperone assemblies that reorganize protein networks under stress. Here, authors reveal how HSP90 phosphorylation drives epichaperome formation, linking this process to cancer cell ...

🧵Follow this thread by Dr. Tanaya Roychowdhury to learn about the intriguing case of #HSP90 - adapted from our recent publication in @natcomms.nature.com (1/8)

#cancer #phosphorylation #epichaperome #conformation #cellstress

www.nature.com/articles/s41...

Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation - Nature Communications Epichaperomes are chaperone assemblies that reorganize protein networks under stress. Here, authors reveal how HSP90 phosphorylation drives epichaperome formation, linking this process to cancer cell ...

To know more about this strange and intriguing case check out our work linked below (8/8)
#phosphorylation #epichaperome #cancer #conformation #cellstress
www.nature.com/articles/s41...

In #cancer, Casein Kinase 2 (CK2) interacts with #HSP90 and puts phosphate groups on Serine 255 and Serine 226 positions of the charged linker region of HSP90 thereby changing its structure or conformation. This dangerous alter ego of HSP90 helps the cancer cells to survive. (7)
#phosphorylation

This switch of HSP90 to "bad" and the formation of the epichaperome makes it so the #epichaperome now aids #cancer. (6)

#Cancer is a multifactorial disease that manifests as a result of chronic cellular stress, a trigger that turns #HSP90 into Mr. Hyde.
Mr. Hyde can now associate with other chaperone protein members and form a gang (high molecular weight assembly) called “epichaperome”. (5)
#epichaperome

In our latest work, now published in
@natcomms.nature.com, we uncover how #HSP90 switches from “good” to “bad” in #cancer. (4)

Heat Shock Protein 90 (HSP90) is a cellular chaperone protein ubiquitously present in human body and is responsible for folding other important proteins in the cell. However, it can exist either as Dr. Jekyll or Mr. Hyde depending on how stressed the cells are. (3) #cellstress #HSP90

Any protein consists of strings of amino acids that fold into distinct different shapes and structures inside the cell depending on the cellular environment. (2)
#proteinstructure #HSP90 #chaperone #cancer #chembio

Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation - Nature Communications Epichaperomes are chaperone assemblies that reorganize protein networks under stress. Here, authors reveal how HSP90 phosphorylation drives epichaperome formation, linking this process to cancer cell ...

🧵Follow this thread by Dr. Tanaya Roychowdhury to learn about the intriguing case of #HSP90 - adapted from our recent publication in @natcomms.nature.com (1/8)

#cancer #phosphorylation #epichaperome #conformation #cellstress

www.nature.com/articles/s41...

🚀 Integrating dfPPI with other omics could reveal comprehensive disease mechanisms, paving the way for groundbreaking discoveries and precision therapeutics across numerous diseases. #MultiOmics #FutureResearch (11/11)

🌐 The open-access dfPPI Platform lets researchers worldwide visualize and analyze dfPPI data interactively, empowering researchers with access to cutting-edge proteomics analysis. #OpenScience #Proteomics

⚕️dfPPI help identify a hyperconnectivity state—an increased level of protein interactions in tumors, where cells become highly sensitive to therapies enhancing their effectiveness. #PrecisionMedicine #CancerTherapy

🔗 Protein connectivity changes detected by dfPPI show minimal correlation with overall protein expression—demonstrating the need to look beyond protein levels to understand true disease biology. #Proteomics #dfPPI

🎗️In cancer cells, dfPPI identifies dysfunctional PPIs critical for malignant behavior—offering insights into novel therapeutic vulnerabilities like mitotic network disruptions. #CancerResearch #Therapeutics

🧠 In Alzheimer’s research, dfPPI unveiled significant changes in protein connectivity, with extensive losses and gains of interactions, highlighting disrupted pathways crucial for memory. #Alzheimers #Neurodegeneration

🖥️ New bioinformatics pipelines now make dfPPI data analytics user-friendly, aiding scientists to map disease-specific protein interactions and pathways without specialized training. #DataScience #Bioinformatics

🔍Specialized #ChemicalProbes are central to dfPPI, capturing dysfunctional interactions—trapping thousands of protein interactors, enabling precise identification of disease-driven interactome changes. #MassSpec #Proteomics (4)

🎯#dfPPI employs protein complexes that form under stress conditions as biological baits, capturing disease-specific changes in protein interactions within native cellular environment. This improves relevance & accuracy of the findings in biological contexts. #Chemoproteomics (3)

Dysfunctional Protein-Protein Interactome (dfPPI) is significantly advancing our understanding of disease by mapping stress-induced changes in protein networks, critical to phenotype and disease manifestation. #SystemsBiology #dfPPI (2)

Introducing dysfunctional Protein-Protein Interactome (dfPPI) – A platform for systems-level protein-protein interaction (PPI) dysfunction investigation in disease Protein-protein interactions (PPIs) play a crucial role in cellular function and disease manifestation, with dysfunctions in PPI networks providing a …

🧵Have you checked out our recent article in
Current Opinion in Structural Biology? Follow this thread by Chiosis Lab postdoc Souparna Chakrabarty
to learn about the Dysfunctional Protein-Protein Interactome (#dfPPI) - a #chemoproteomic platform www.sciencedirect.com/science/arti... 🧵(1/11)

💫Preprint available now! Our most recent research on #Alzheimers and #epichaperomes is below. Read to find out how #epichaperomes are key mediators of molecular collapse in #AD & what avenues are promising for disease-modifying #therapies🧠
www.researchsquare.com/article/rs-5...