Martin
@mamueller.bsky.social
170 followers 550 following 2 posts
Postdoc, interested in translation regulation and mRNA decay
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Reposted by Martin
johntngo.bsky.social
🚀 Our new paper is out @natmethods.nature.com!

Kuffer & Marzilli engineered conditionally stable MS2 & PP7 coat proteins (dMCP & dPCP) that degrade unless bound to RNA, enabling ultra–low-background, single-mRNA imaging in live cells.

🔗 www.nature.com/articles/s41...
🧬 www.addgene.org/John_Ngo/
Reposted by Martin
pelletfraction.bsky.social
Why are α-synuclein aggregates in Parkinson’s disease (PD) toxic at the cell biological level?

Our new study shows that α-syn fibrils hijack the ESCRT membrane repair system, triggering a feedback loop that worsens aggregation.

You can find it at: authors.elsevier.com/sd/article/S...
ScienceDirect.com | Science, health and medical journals, full text articles and books.
authors.elsevier.com
Reposted by Martin
mpibiochem.bsky.social
Structural & functional analysis revealed that the extracellular #chaperone #clusterin functions through two tails in preventing protein aggregation.

❕Paper: www.nature.com/articles/s41...
❕Press Release: www.biochem.mpg.de/structure-of...

#Alzheimers @natsmb.nature.com @pyustecheca.bsky.social
Reposted by Martin
pyustecheca.bsky.social
Curious about the structure and functional analysis of one of the most abundant and enigmatic extracellular #chaperones and one of the highest genetic risk factor for developing late onset #Alzheimer’s disease? Check out our paper on Clusterin/ApoJ!
#proteostasis #apolipoprotein
rdcu.be/ezRLv
Structural analyses define the molecular basis of clusterin chaperone function
Nature Structural & Molecular Biology - The authors reveal a three-domain architecture of glycoprotein clusterin and show that the hydrophobic tails are crucial for clusterin’s functions...
rdcu.be
Reposted by Martin
christinemayr.bsky.social
New paper:
More than 2700 human 3′UTRs are highly conserved. These 3′UTRs are essential components in mRNA templates, as their deletion decreases protein activity without changing protein abundance. Highly conserved 3′UTRs help the folding of proteins with long IDRs.

www.biorxiv.org/content/10.1...
mRNA 3′UTRs chaperone intrinsically disordered regions to control protein activity
More than 2,700 human mRNA 3′UTRs have hundreds of highly conserved (HC) nucleotides, but their biological roles are unclear. Here, we show that mRNAs with HC 3′UTRs mostly encode proteins with long intrinsically disordered regions (IDRs), including MYC, UTX, and JMJD3. These proteins are only fully active when translated from mRNA templates that include their 3′UTRs, raising the possibility of functional interactions between 3′UTRs and IDRs. Rather than affecting protein abundance or localization, we find that HC 3′UTRs control transcriptional or histone demethylase activity through co-translationally determined protein oligomerization states that are kinetically stable. 3′UTR-dependent changes in protein folding require mRNA-IDR interactions, suggesting that mRNAs act as IDR chaperones. These mRNAs are multivalent, a biophysical RNA feature that enables their translation in network-like condensates, which provide favorable folding environments for proteins with long IDRs. These data indicate that the coding sequence is insufficient for the biogenesis of biologically active conformations of IDR-containing proteins and that RNA can catalyze protein folding. ### Competing Interest Statement The authors have declared no competing interest. Pershing Square Foundation, https://ror.org/04tce9s05 G. Harold & Leila Y. Mathers Foundation National Institutes of Health, DP1GM123454, R35GM144046 Memorial Sloan Kettering Cancer Center, https://ror.org/02yrq0923, P30 CA008748
www.biorxiv.org
Reposted by Martin
davidbalchin.bsky.social
New from our lab @crick.ac.uk, in collaboration with the Enchev and Bukau labs.
By studying a protein that is difficult to fold, we discover fascinating new mechanisms by which the ribosome supports protein biogenesis.
www.biorxiv.org/content/10.1...
Reposted by Martin
beckmannlab.bsky.social
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. 👇👇👇
Reposted by Martin
embojournal.org
How does an unusual heptameric AAA-ATPase translocate fully-folded Rieske protein across the inner mitochondrial membrane?
Cryo-EM & functional data by Roland Beckmann and coworkers show how Bcs1 alternates between different states during its translocation activity.
www.embopress.org/doi/full/10....
Reposted by Martin
doc-jlmeier.bsky.social
Excited to share this one! We developed an in vivo model for specific manipulation of transfer RNA acetylation and found it serves as a sentinel modification whose loss causes ribosome stalling and stress signaling. Implications for a genetic disorder and cancer.

www.science.org/doi/10.1126/...
Transfer RNA acetylation regulates in vivo mammalian stress signaling
An ancient tRNA modification is used by mammalian cells to coordinate protein translation and adaptive signaling.
www.science.org
Reposted by Martin
jakobfarnung.bsky.social
🎉Super excited to share our story on how the substrate receptor FBXO31 functions as a quality control factor by recognizing amides. This has been an amazing collaboration between Bode lab and @jcornlab.bsky.social. Special shutout goes to @matthiasmuhar.bsky.social www.nature.com/articles/s41...
C-terminal amides mark proteins for degradation via SCF–FBXO31 - Nature
SCF–FBXO31 scans proteins for C-terminal amidation and marks them for subsequent proteasomal degradation.
www.nature.com
Reposted by Martin
johnrubinstein.bsky.social
We are hosting a cryo-EM grid nanofabrication workshop on 28 April 2025, as part of the Canadian Cryo-EM Nexus (ccemn.ca).
Learn how to make holey gold or holey carbon grids in your own laboratory!
Space is limited, so please apply at web.cvent.com/event/ee88ac...
Reposted by Martin
mrclmb.bsky.social
Huping Wang and Manu Hegde, in @cellbiol-mrclmb.bsky.social have found a factor that accelerates protein deliveries to the endoplasmic reticulum

Click here to read more about it: www2.mrc-lmb.cam.ac.uk/discovery-of...

#LMBResearch
Model depicting the early steps during production of a membrane protein
Reposted by Martin
clausenlab.bsky.social
#TGIF-JC TMEM208 - a protein to remember

amazing work from the Hegde lab showing that this long-overlooked protein helps SRP to properly release its cargo at the ER membrane, ensuring smooth translocation. especially important for multipass membrane proteins.

www.science.org/doi/10.1126/...
Identification of a factor that accelerates substrate release from the signal recognition particle
The eukaryotic signal recognition particle (SRP) cotranslationally recognizes the first hydrophobic segment of nascent secretory and membrane proteins and delivers them to a receptor at the endoplasmi...
www.science.org
Reposted by Martin
Reposted by Martin
erzbergerlab.bsky.social
Our latest paper, a fantastic collaboration with the Mendell Lab, is out. Great work by Xiaoqiang Zhu and Victor Cruz. We uncover how tRNA structural features in the ribosomal P-site modulate co-translational mRNA decay by the CCR4-NOT complex. #RNAsky #RNAbiology #translation #ribosome #cryoEM 1/5
www.science.org