Briggs Group

An amazing study from @chlandalab.bsky.social - a lot of new insights from these beautiful tomograms!

Providing order amongst constant traffic: #LMBResearch from Sean Munro (@cellbiol-mrclmb.bsky.social) with John Briggs (@mpibiochem.bsky.social) reveals how GOLPH3 allows COPI vesicles to distinguish between Golgi residents & ER-bound proteins.
Read more: www2.mrc-lmb.cam.ac.uk/protein-sort...

The mechanistic basis of cargo selection during Golgi maturation Resident proteins of the Golgi recycle in vesicles and the protein GOLPH3 enables the COPI vesicle coat to accomplish this.

The mechanistic basis of cargo selection during Golgi maturation. From Rebecca Taylor, @katciazynska.bsky.social, @jggkaufman.bsky.social & @grigorytagiltsev.bsky.social at @mpibiochem.bsky.social with David Owen and Sean Munro's group @cellbiol-mrclmb.bsky.social | www.science.org/doi/10.1126/...

Apply now! Apply to become a Max Planck Research Group Leader. Max Planck Research Groups - Announcement 2024.

Do you want to start your own research group? The current call for Max Planck Research Group Leaders is open until October 14th.

www.mpg.de/career/max-p...

Open Call for Expressions of Interest in Max Planck Directorships: Expressions of interest can be submitted until 31 October 2025.

Director at Max Planck - a unique position! The Open Call for Expressions of Interest in Max Planck Directorships is open now and can be submitted by the 31st of October 2025. ➡️ mpg.de/directors - Please share the Open Call among potential candidates.

A comparison of the structures of dArc1 (capsid: 6TAP; pentamer: 6TAR), the retrovirus HIV (capsid: 3J3Q; pentamer: 7URN), and the retrotransposon Ty3 (6R24). Pentamers are shown in orange, and hexamers in yellow in the upper panel. In the lower panel, pentamers are shown with monomers colored in different shades of orange.

How did a brain gene end up behaving like a virus? Research has shown that there is an evolutionary connection between Arc, retroviruses, and virus-like genetic elements called retrotransposons.
More at Molecule of the Month: pdb101.rcsb.org/motm...

Congratulations @tbharat-lab.bsky.social !

We’ve uncovered Asgard chromatin structures formed by a Hodarchaeal histone : closed hypernucleosome conserved in archaea and an open form resembling the H3-H4 eukaryotic octasome. Fantastic work by @harshranawat.bsky.social!
www.biorxiv.org/content/10.1...
#Chromatin #Asgard #Archaea #cryoEM

Thrilled to share these experiments on shaping focused ion beams to explore different ways of milling. Here, we explore using different beam geometries to generate cellular thin sections/lamellae. The video shows elongating the beam on a charging spot burn www.biorxiv.org/content/10.1...

Our work on HIV-1 matrix, led by James Stacey and @dhrebik.bsky.social, is in this week's @nature.com. Extended explanatory video from @margotriggi.bsky.social.

www.nature.com/articles/s41...

Mechanisms of COPII coat assembly and cargo recognition in the secretory pathway - Nature Reviews Molecular Cell Biology Coat protein complex II (COPII) subunits assemble to form membrane transport carriers at ER exit sites, thereby concentrating secretory cargoes and facilitating their transport to the Golgi. This Revi...

New #Review 🥳

@dr-downes.bsky.social and @giuliazanetti.bsky.social discuss recent findings on how #COPII particles assemble and recognise their cargo as part of the #SecretoryPathway

🔗 go.nature.com/3XJHHmy

Repost appreciated:

Open #PhDposition in structural virology in my group! Join us in Umeå, 🇸🇪 to uncover how arboviruses remodel the cellular interior. In situ #cryoET combined with #virology, #cellbiology, and #biophysics.

Deadline 4 May. More info: www.carlsonlab.se/join/

Our #cryoEM technology group with scientists from @mpibp.bsky.social and @viennabiocenter.bsky.social, used #cryoET to capture retrotransposons in action, resolving copia in #fruitflies at sub-nanometer resolution inside cells.

❕Publication @cellpress.bsky.social: www.cell.com/cell/fulltex...

The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation - Nature A study reports that the structural maturation of the matrix domain of the Gag protein of HIV-1 is induced by the proteolytic release and binding of the spacer peptide SP2.

Without SP2, HIV-1 fuses more slowly with target cells. We worked with Kräusslich and Müller labs @uniheidelberg.bsky.social,
@wmothes.bsky.social at @yalemicropath.bsky.social, Robert Dick @emorydeptofmed.bsky.social and Kun Qu.
Read the full paper @nature.com here: www.nature.com/articles/s41...

HIV-1 spacer peptide 2 binds to a pocket on the side of the matrix protein

James Stacey and @dhrebik.bsky.social generated high-resolution structures of matrix within virus particles by #cryoEM, finding SP2 bound to a pocket on matrix (we previously thought the ligand was a lipid):

Mature #HIV-1 contains >2000 copies of “spacer peptide 2”, but we didn’t know why. We now see that SP2 binds the matrix protein and triggers the change into its mature arrangement. Summary video from @margotriggi.bsky.social