Max Gemmer
@MaxGemmer
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PhD student at Utrecht University. Interested in Cryo-ET, protein biogenesis, endoplasmic reticulum. #TeamTomo #CryoEM #SciArt
Utrecht, Netherlands
Joined April 2021
Very happy to share our recent work on protein biogenesis at the ER membrane. We analyzed 150,000 ribosomes from 1000+ tomograms of ER-derived vesicles to visualize ribosome intermediates and their downstream translocon machinery. 1/ #TeamTomo #CryoEM
https://t.co/MXeQ598RvZ
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You always wanted a book on cryo- electron tomography, written by the leading experts in the field? I have good news-You can now pre- order this book, edited by the one and only @FriedrichForst1 and myself!
link.springer.com
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Muyuan has been working on this for some time, it's cool to see a manuscript: How to create full, atomic resolution scenes of biomolecules in Unreal Engine and fly around them in real-time. Really cool stuff with untapped potential. https://t.co/dWQ6nhRnNJ
https://t.co/oRDsvwECgj
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Happy to report our new structure of Sec61 and the TRAP complex out now in @emboreports! This has been a nice group effort with us @BIOTECH_UH and with @JuhaHuiskonen and @LHapponen @lunduniversity. https://t.co/iRd0CzMy6L
embopress.org
image image The structure of the heterotetrameric TRAP complex reveals the mode of interaction with the ribosome and the Sec61 protein translocation channel. Molecular dynamics simulations suggest...
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9 | Big thanks to @ChailletMarten, @FriedrichForst1, and the rest of our team for their contributions. The full raw data set of unperturbed ER-derived vesicles from this and our previous paper is now also available online
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8 | The function and interplay between TRAP, NOMO, and NCLN remains largely obscure. The architecture of the BOS complex (NCLN-NOMO) and its interaction with the insertase EMC was now characterized by the @voorheeslab. Check out their paper, too! https://t.co/VNqE1sKuEo
biorxiv.org
Mammalian membrane proteins perform essential physiologic functions that rely on their accurate insertion and folding at the endoplasmic reticulum (ER). Using forward and arrayed genetic screens, we...
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7 | Finally we visualize the interaction of TRAP and the multipass translocon. Based on our locally refined reconstruction, Alphafold models, and previous studies we show that TRAP associates with NOMO, a subunit of the BOS complex that was previously not resolved
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6 | We believe that PAT is recruited only in the presence of nascent substrate, while TRAP may dissociate in order to avoid insertion of topogenic sequences into the lateral gate, thus favoring insertion via the specialized multipass translocon at the back side instead
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5 | This now allows us to study the distribution of PAT and TRAP in context of translation activity. Our results indicate that PAT associates preferably with active multipass translocons, while TRAP is preferentially bound to the inactive translocon
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4 | For functional context, we again reviewed our previous results. Back then, we sorted ER-bound ribosomes into actively elongating and hibernating particles https://t.co/FXCkjVhMIS
We identified 8 elongating and 2 hibernating intermediate states ranging from 4-8 Å resolution. High abundance of actively elongating ribosomes (90%) indicate only little sample prep effects. Compatible with in situ data, we found 66% of ribosomes bound to (elongation)factors. 2/
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3 | In addition, we now show that TRAP and PAT are both variable components of the multipass translocon. PAT was shown to chaperone nascent TMHs at the backside of the translocon, while TRAP is known to support signal peptide insertion into the lateral gate at the front side
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2 | Quick recap: Earlier this year we found that the multipass translocon is a constitutive variant in ER-derived vesicles from HEK293F cells using cryo-ET https://t.co/HMK8KCDtqU
Very happy to share our recent work on protein biogenesis at the ER membrane. We analyzed 150,000 ribosomes from 1000+ tomograms of ER-derived vesicles to visualize ribosome intermediates and their downstream translocon machinery. 1/ #TeamTomo #CryoEM
https://t.co/MXeQ598RvZ
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1 | Multispanning membrane proteins are co-translationally inserted by the ribosome-bound multipass translocon; a molecular ensemble composed of the GEL, PAT, and BOS complex. Nascent multi-transmembrane helices (TMHs) are inserted into the backside of the Sec61 channel
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How is the biogenesis machinery organized to produce multispanning membrane in humans? In our most recent preprint, we characterize the composition of the multipass translocon in its native membrane environment using cryo-ET. 🧵 #TeamTomo #cryoEM
https://t.co/SyLSTqEAWs
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We developed "DeepFIBing" - a new strategy to create #cryoFIB-lamellae for #cryoET in any depth of very large cells - this also works for tissue. If you want to know more, have a look into our publication in CELL with @jentoft_ida and @SchuhLab. #teamtomo
https://t.co/O4qWvG4uiT
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Want to learn how to create stunning scientific visualizations in #b3d? Check out @bradyajohnston's molecular nodes and @luminous_lab's tutorials on YouTube! #SciArt
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I successfully defended my PhD thesis on protein biogenesis last week. I am really grateful to my supervisor @FriedrichForst1, colleagues and friends for this wonderful experience! In particular Juliette Fedry and @ChailletMarten who significantly contributed to our projects.
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Great symposium to honor the opening of the cryoEM facility in Berlin! Thank you for the invitation @MishaKudryashev, Christian Spahn and Christoph Diebolder. Happy invited speakers Helen Saibil, @FriedrichForst1 and Kay Grünewald
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Excited to share our in situ #CryoET story on the effect of a top antimalarial drug candidate on the translational landscape in #CryoFIB-milled malaria parasites! So proud of this massive team effort with @leonie_anton @_wenjing_cheng_ @mehsehret @davwcbb🥰#officially #teamtomo
In situ cryoET reveals inhibitor-induced perturbations in Pf80S GTPase interactions https://t.co/g1BGJFdVRL
#bioRxiv
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🧵[1/6] We achieve high-confidence localization of a wide range of macromolecular complexes, their subunits, and functional substates through 3D template matching (TM) for #CryoET. This allows us to capture vaults transporting ribosomal cargo in situ!🤯 https://t.co/c00EY6NiRu
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Abstract submission is now open! Register for this EMBL workshop on the application of cryo-EM in industry and academia
embl.org
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