@FrydmanLab

A lab at Stanford University studying protein biogenesis, folding, and aggregation in health and disease. Tweets by lab members.

 Stanford, CA
web.stanford.edu/group/frydman/web/
Joined February 2020
  • Tweets195
  • Following131
  • Followers1.3K
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Another great story from Jae Ho Lee in the lab: a new concept in cotranslational proteostasis-ribosome communication via chaperoneNAC. An exciting collaboration with Elke Deuerling's lab @DeuerlingLab and Marina Rodnina's lab biorxiv.org/content/10.1101/…

NAC controls nascent chain fate through tunnel sensing and chaperone action

The nascent polypeptide-associated complex (NAC) is a conserved ribosome-bound factor with essential yet incompletely understood roles in protein biogenesis. Here, we show that NAC is a multifaceted...

biorxiv.org
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New exciting work from Jae Ho Lee in our lab, in a fantastic collaboration with Alessandro Ori @AOri_lab and Alessandro Cellerino @Alessan82703458 on why and how the brain ages and becomes vulnerable to neurodegenerative diseases science.org/doi/10.1126/scie…

Altered translation elongation contributes to key hallmarks of aging in the killifish brain

Aging is a major risk factor for neurodegeneration and is characterized by diverse cellular and molecular hallmarks. To understand the origin of these hallmarks, we studied the effects of aging on...

science.org
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Paging @NIHDirector_Jay . Is abruptly cutting these grants going to "make America healthy again"?
Uri Manor
@manorlaboratory6 Jul 2025
My lab’s 5-year NIH R01 grant, awarded to study gene therapy for hearing loss, was abruptly terminated. I want to share how this action has been incredibly harmful and disruptive, not just to my lab, but to the scientific process itself. 1/15
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Triglycerides are an important fuel reserve for synapse function in the brain go.nature.com/4nvjk7k

Triglycerides are an important fuel reserve for synapse function in the brain

Nature Metabolism - Kumar et al. show that under glucose-depleted conditions, neurons can use fatty acids as an alternative source of energy to support synaptic function.

nature.com
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I stand with dozens of other biopharma leaders highlighting the potential catastrophic effects of proposed research cuts on bringing innovation to patients! statnews.com/2025/06/27/biot…

Proposed cuts could have ‘catastrophic effect,’ 110 biomedical, health sciences industry leaders...

Proposed cuts will have “a catastrophic effect on the advancement of biomedical and biotechnology capabilities in the United States,” more than 100 leaders of biomedical/health sciences companies...

statnews.com
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My NIDA grant renewal is almost 2 months late and I’m going to have to start firing my students and staff. Not a lot of transformation to be had in my lab.
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Frydman Lab retweeted
Eran Segal@segal_eran15 Jun 2025
Our lab at the Weizmann Institute was hit tonight by Iran We will rebuild and return 💪
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It was a pleasure to participate in the "Protein folding & Chaperones" platform session this morning in #bps2025 sharing our story from the @FrydmanLab about TRiC mutations and their link with brain malformations. A session with a nice mix of cool stories focused protein folding
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Closing an unforgettable chapter at Stanford. Grateful for the science, the growth, and the incredible people who shaped this journey—especially Judith, with whom I had the privilege of doing great science. This place and its people will always mean a lot to me. Very excited!
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3) Two surprises that could only be revealed by cryoET raise new cool future questions (I) It uncovered a new cofactor, PDCD5 which binds to ALL open TRiC complexes (and was missed by biochemical studies) and (II) closed TRiC forms stereotypic clusters of mysterious function.
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2) The MS also quantified TRiC-Prefoldin cooperation in vivo. Importantly it establishes that closed TRiC engages in specific interactions with quasi-folded substrate folding intermediates in its closed folding chamber, which is clearly NOT an "Anfinsen cage"
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Check out our MS describing the in vivo cycle of chaperonin TRiC/CCT, in a wonderful collaboration with Martin Beck's lab: nature.com/articles/s41586-0… 1) The study established TRiC's important function in folding newly translated proteins and defines its ATP-driven cycle

In situ analysis reveals the TRiC duty cycle and PDCD5 as an open-state cofactor

Nature - TRiC functions at near full occupancy to fold newly synthesized proteins inside cells.

nature.com
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A really nice piece on our recent study: med.stanford.edu/news/all-ne…

Rare, mysterious brain malformations in children linked to protein misfolding, study finds

Mutations in a complex that helps proteins fold correctly are tied to developmental disorders that include seizures and intellectual disability, Stanford Medicine-led research has found.

med.stanford.edu
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4. The concept of chaperonin function as central in brain development is a new paradigm opening the door to many additional mysteries. Thanks to all: Ingo,  Miriam, Stephen, Florian, Piere for the fun collaboration and to Manu Sharma for the highlight: science.org/doi/10.1126/scie…

Some brain disorders are “chaperonopathies”

Mutations that impair a protein-folding chaperone can lead to brain malformations

science.org
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3. From a clinical perspective, these patients with "TRiCopathies" may be at an extreme end of a spectrum, with frequent but less-severe TRiC genetic variants causing milder intellectual disability and seizure phenotypes.
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2. Despite its ubiquitous expression, de novo mutations in seven out of the eight CCT-genes led to brain malformations, intellectual disability, and seizures in a total of 22 patients. Thus, insufficient TRiC folding capacity becomes a bottleneck in brain development.
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1. Check out our latest and exciting MS describing a new class of neurodevelopmental diseases caused by mutations in most subunits of the chaperonin TRiC/CCT. science.org/doi/10.1126/scie… (part 1 of series)

Brain malformations and seizures by impaired chaperonin function of TRiC

Malformations of the brain are common and vary in severity, from negligible to potentially fatal. Their causes have not been fully elucidated. Here, we report pathogenic variants in the core protei...

science.org
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5. We hope others use this robust strategy for reliably detecting pausing events even in low coverage data. Our approach may open the way to understand translation dynamics in rare and valuable samples, such as donor tissues or single cell analyses.
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4. iii) We identify nascent chain sequences in the exit tunnel that contribute to sequence-specific pausing iv) We find that ribosome collisions arise from an elongation rate mismatch of proximal ribosomes translating sequences with opposite elongation rates.
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3. i) We dissect the interdependence and distinct contributions of amino acid properties and tRNA abundance on elongation pausing ii) We find that competition between tRNAs leads to wobble pairing playing a preeminent role in decoding the translatome
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