Thibault Mayor
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cellsandprots.bsky.social
Thibault Mayor
@cellsandprots.bsky.social
Prof of Biochemistry & Molecular Biology at @ubc and @msl Our team focuses on proteostasis and yeast cell biofactories
❤️ ubiquitin, chaperones & proteomics
💙 outdoor, repast, electro-rock & traveling 🇨🇭🇨🇦

https://mayor51.wixsite.com/mayorlab
Haha I used to read this🇨🇭newspaper back then and my mom still has a subscription. Fun read on a not so fun topic
November 1, 2025 at 4:11 PM
4 months after biorxiv submission sounds like a smooth ride - congrats
April 5, 2025 at 12:45 AM
You almost look like Leonard on that picture ;-)

Happy birthday- enjoy the rest of the trip
January 27, 2025 at 3:32 AM
Many people contributed to this project led by @hthrbaker.bsky.social with help from @shriyakamat.bsky.social and great collaborators in @miketilapia.bsky.social and Brian Raught's labs

The illustration was created by @taniodraws.bsky.social our go-to freelance artist for summarizing our studies.
January 10, 2025 at 5:10 PM
One limitation of our study is the use of rapidly dividing cells, where the protein homeostasis network likely differs from that in differentiated cells with lower protein production. Despite our efforts, we have yet to identify the E3 ligase involved—but we’re not giving up, so stay tuned!
January 10, 2025 at 5:10 PM
In this case, the disease-associated mutation increases interaction with the DNAJA2 chaperone, which appear to be dispensable for the folding of the wild-type protein. This interaction delays the proteolysis of the mutant protein, potentially buffering its deleterious effects.
January 10, 2025 at 5:10 PM
Using BioID, we identified chaperones, including the co-chaperone DNAJA2, that interact more with the unstable thiopurine S-methyltransferase (TPMT) variant than the wild type. DNAJA2 deletion accelerates degradation of the mutated TPMT but does not affect the wild-type protein
January 10, 2025 at 5:10 PM
Many disease-associated mutations are missense mutations causing single amino acid changes that signal proteins for degradation. We surveyed 18 unstable variants from 13 cytosolic proteins and found that all but one are at least partially degraded via proteasome- and ubiquitin-dependent pathways.
January 10, 2025 at 5:10 PM
Congratulations to the whole team!
December 21, 2024 at 1:53 AM
🤔 a lot of us will have to leave. Yes I am co-author on a MPDI journal 😬 But yeah if a see a lot of these journals in a CV, it will dampen my enthusiasm for an application

We first need to better educate our trainees about the issue (e.g. does your grad program cover the topic in a course?)
December 12, 2024 at 4:09 PM