Jay Brito Querido

Jay Brito Querido

@jbquerido.bsky.social

Assistant Professor at the University of Michigan Medical School and @umlifesciences.bsky.social #cryoEM #RNA #Ribosomes #RNAsky #RNABiology #Science https://www.lsi.umich.edu/science/our-labs/brito-querido-lab

3.4K followers1.4K following14 posts

Jay Brito Querido reposted

I'm thrilled to anounce that our latest study on ALS/FTD neurodegenerative diseases has been published. Very proud to be part of this excting project. Many thanks to Clotilde Lagier Tourenne for an amazing longlasting and fruitfull collaboration, #ALS #FTD #Ribosomes www.science.org/doi/10.1126/...

science.orgBlocking RAN translation without altering repeat RNAs rescues C9ORF72-related ALS and FTD phenotypesGGGGCC (G4C2) repeat expansion in C9ORF72 is the most common genetic cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Toxicity is thought to result from the accumulation...

Jay Brito Querido reposted

Excited to share a new chapter of my scientific journey in Chris Russo's group — developing a way to freeze proteins faster than they diffuse, paving the way for cryo-EM without air–water interface damage.

Chris Russo and Anastasiia Gusach have developed a new method to prepare #cryoEM samples that avoids protein damage during freezing Read more: www2.mrc-lmb.cam.ac.uk/a-new-method... #LMBResearch

Jay Brito Querido reposted

Finally out! I’m thrilled to share our new paper (Wolin et al., Cell 2025). This paper describes SPIDR, a high-throughput method for mapping RBP binding sites. By combining #SPIDR with #cryoEM, we identified the exact binding site of LARP1 within the #mRNA channel of the 40S ribosomal subunit.

Jay Brito Querido reposted

Jay Brito Querido reposted

Jay Brito Querido reposted

Jay Brito Querido reposted

Jay Brito Querido reposted

I’m thrilled to share my very first first-author preprint and our lab’s latest work💫 We discovered a novel role for eIF2A in ribosome-associated quality control (RQC), challenging decades-old assumptions about its enigmatic function in translation initiation. Check it out to learn more! ⭐️ #RNA

Sendoel Lab@sendoellab.bsky.social

Identified in the 1970s, the precise molecular function of the alternative initiation factor eIF2A has remained unclear. Here, we map its interactome and uncover a surprising role in ribosome-associated quality control (RQC) upon ribosome stalling. 1/x www.biorxiv.org/content/10.1...

Jay Brito Querido reposted

Jay Brito Querido reposted

We are happy to share that our snR30 story is finally out in @natureportfolio.nature.com 🥳 We report the first structure of a H/ACA snoRNP acting in ribosome synthesis thereby providing a detailed structural and biochemical view of the snR30 snoRNP guiding local 18S rRNA subdomain folding. 👇👇👇

Jay Brito Querido reposted

Jay Brito Querido reposted

Hello Bluesky! 🌤️ We're on the Molecular Cell cover! How are ribosome levels adjusted? Stm1 not only protects ribosomes from degradation, it also promotes their biogenesis in nutrient-rich conditions. Two roles, one protein - tuned by nutrient availability. 🔗 www.cell.com/molecular-ce...

cell.comStm1 regulates Ifh1 activity revealing crosstalk between ribosome biogenesis and ribosome dormancyRibosome abundance is balanced by production and degradation. Bianco et al. discover that the hibernation factor Stm1 has a dual role in ribosome homeostasis. Stm1 promotes ribosome biogenesis during ...
Molecular Cell@cp-molcell.bsky.social

Read the latest issue here: www.cell.com/molecular-ce...

Jay Brito Querido reposted

You want to start tomography? Solve structures inside cells? Reach Nyquist 😳 ? @phaips.vd.st and I have a website for you! tomoguide.github.io You'll find a tutorial on how to reconstruct tomograms, pick particles and do subtomogram averaging, using different software! Hope it will be useful !

Hey #TeamTomo, Ever been in need of a tutorial about the fundamentals of cryo-electron tomography? From preprocessing raw frames to high-res subtomogram averaging? That's why @florentwaltz.bsky.social and I made this website! tomoguide.github.io Follow the thread 1 /🧵 #CryoET #CryoEM 🔬🧪

Jay Brito Querido reposted

In our newly published study we show that the proline-rich antimicrobial peptide (PrAMP) Bac5 has a distinct mode of interaction with the ribosome compared to other PrAMPs…https://academic.oup.com/nar/article/53/8/gkaf324/8126264

academic.oup.comThe structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1–17)Abstract. Proline-rich antimicrobial peptides (PrAMPs) are produced as part of the innate immune response of animals, insects, and plants. The well-charact

Jay Brito Querido reposted

Watching Sven elucidate this mechanism from an unbiased screen onwards has been one of my favorite experiences as a PI. In these challenging times for science at Harvard, it reminds me of the sheer joy of doing science and making discoveries.

Sven Lange@sven-m-lange.bsky.social

How do cells keep their cilia “clean” and functional? Our new study uncovers a conserved mechanism for retrieving polyubiquitinated proteins from #cilia – a process essential for cellular signaling and health. #cellbiology #ciliopathy #ubiquitin #IFT 🧵👇 1/n

biorxiv.orgA conserved mechanism for the retrieval of polyubiquitinated proteins from ciliaThe temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using a multidisciplinary approach, we demonstrate that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts Hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis, and demonstrate how structural changes in IFT trains achieve cargo selectivity. ### Competing Interest Statement The authors have declared no competing interest. Sara Elizabeth O'Brien Trust Postdoctoral Fellowship awarded through the Charles A. King Trust Postdoctoral Research Fellowship Program, , 8460873-01 Richard and Susan Smith Family Foundation, https://ror.org/05j95n956, National Institute of General Medical Sciences (NIGMS), , R01GM141109, R01GM143183

Jay Brito Querido reposted

Jay Brito Querido reposted

I am happy to share the latest paper from the lab. We detail a tripartite cell-free translation system based on the separation of mRNAs, ribosomes and ribosome-depleted cytoplasmic lysate from human cells, allowing for flexible reconstitution of translation reaction. #RNA #Ribosome

Jay Brito Querido reposted

Fresh off the press…our latest study on the Structure of a Gcn2 dimer in complex with the large 60S ribosomal subunit | great collaboration with inada and Zaher labs. Data collected by Bertrand Beckert at the DCI EPFL www.pnas.org/doi/10.1073/...

pnas.orgStructure of a Gcn2 dimer in complex with the large 60S ribosomal subunit | PNASThe integrated stress response (ISR) is a central signaling network that enables eukaryotic cells to respond to a variety of different environmenta...

Congratulations to PhD student Brenna Saladin from my lab on receiving the NSF GRFP! And kudos to PhD students Suada Leskaj and Rodolfo Murguia for being recognized with Honorable Mentions! #RNA #CryoEM #Science

Jay Brito Querido reposted

New preprint drop! Check out work from @jimmy-ly.bsky.social et al for how protein isoforms generated by alternate translation initiation create dual localization, contribute to mitochondrial function, and are mutated in disease. "Blue-tutorial" thread below. www.biorxiv.org/content/10.1...

biorxiv.orgAlternative start codon selection shapes mitochondrial function during evolution, homeostasis, and diseaseMitochondrial endosymbiosis was a pivotal event in eukaryotic evolution, requiring core proteins to adapt to function both within the mitochondria and in the host cell. Here, we systematically profile...
Iain Cheeseman@iaincheeseman.bsky.social

Countdown to an epic new pre-print. Mitochondria are cells within our cells. They need the same core activities - replication, transcription, translation. How do cells enable these diverse activities in both compartments? We uncover an unexpected + broad strategy with ancient origins. Stay tuned!

Jay Brito Querido reposted

Jay Brito Querido reposted

We're on the cover of @science.org this week. Awesome work by @florentwaltz.bsky.social. #CryoET is reaching crazy resolutions inside cells, and this is just the beginning. Fantastic interpretation of the proton motive force by @verenaresch.bsky.social. Always a pleasure making #SciArt with you!🧪🧶🧬🌾

Science Magazine@science.org

In a new Science study, cryo–electron tomography captures the in-cell architecture of the mitochondrial respiratory chain, illuminating how the coordinated action of molecular machines drives life’s fundamental energy conversion. Learn more in this week's issue: scim.ag/3FA3Ygq

Jay Brito Querido reposted

The insides of microtubules of motile cilia and flagella are coated in proteins - but are they all important for motility? Our latest collaborative study addresses this question using trypanosomatids as model organisms. Matt explains more below:

Matt Doran@matthdoran.bsky.social

I am super excited to share our latest work on the structures of doublet microtubules from trypanosomatid parasites, the causative agents of leishmaniasis, Chagas disease, and African sleeping sickness. tinyurl.com/48sh3xn5

Jay Brito Querido reposted

Jay Brito Querido reposted

What do Europeans think of science and technology? - 83% believe science and tech have a positive impact, - 67% say science makes life easier, healthier and more comfortable, - 58% want to learn more about scientific advances. Find out more in the new Eurobarometer. ec.europa.eu/commission/p...

ec.europa.euEuropeans strongly support science and technology according to new Eurobarometer surveyThe latest Eurobarometer survey on ‘European citizens' knowledge and attitudes towards science and technology' released today shows more than 8 in 10 citizens (83%) think that the overall influence of...