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Reposted by Vanni Lab at UNIFR, Switzerland

Claudia Bank @cbank.bsky.social · 1d

Please spread the word! 10 days left to apply for this #sciencejobs as Assistant Professor Tenure Track in Quantitative Cell Biology 👩‍🔬
@izb-unibern.bsky.social @unibe.ch! ohws.prospective.ch/public/v1/jo...
#QueerInSTEM #DisabledInSTEM #BlackInSTEM #WomenInSTEM #CarersInSTEM #AcademicSky #HigherED

Uni Bern: Assistant Professor with tenure-track for Quantitative Cell Biology

Start date of employment: anticipated for August 2027

ohws.prospective.ch

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Reposted by Vanni Lab at UNIFR, Switzerland

André Nadler @nadlerlab.bsky.social · 29d

This is an really amazing opportunity. If you get it, you can essentially pick you institute. The package really is rather competitive.

Max-Planck-Gesellschaft @maxplanck.de · 29d

Springboard for an international scientific career! 🧬🧪🔭⚛️🧠🌱 Call for #MaxPlanckResearchGroups launched; applications are possible until October 14, 2025 www.mpg.de/max-planck-r... #ScienceCareer

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Reposted by Vanni Lab at UNIFR, Switzerland

Suayb Üstün @suaybuestuen.bsky.social · Aug 22

Job alert 📣 Our faculty looks for a Junior Professor W1 with tt to W2 in Membrane Biology! We are looking for #ECRs working on membrane biogenesis,contact sites,composition & other aspects of membranes in 🌱 and other organisms! DM me if you need more details!

jobs.ruhr-uni-bochum.de/jobposting/f...

W1TTW2 Professorship in Membrane Biology (m/f/d)

jobs.ruhr-uni-bochum.de

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Reposted by Vanni Lab at UNIFR, Switzerland

IGBMC @igbmc.bsky.social · Aug 21

Ne manquez pas le 20e GERLI International Lipid Meeting, Strasbourg, 3-5 nov 2025

Rejoignez chercheurs et experts pour explorer les dernières avancées en biologie des lipides, assistez à des conférences, posters et prix scientifiques !

Plus d'info : : www.gerli.com/congres/welc...

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Aug 21

Well...for once I can repost/like a paper I read very carefully 😆

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Aug 21

Congratulations André and team. Very very nice work!

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Reposted by Vanni Lab at UNIFR, Switzerland

Milena Schuhmacher @mschuhmacher.bsky.social · Aug 12

We are hiring!

If you are looking for a postdoc position and you are interested in signaling lipids and proteomics, come join us in beautiful Switzerland!

More information on www.epfl.ch/labs/gr-schu...

Open positions

GR-SCHUHMACHER

www.epfl.ch

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Aug 7

All trajectories and in Zenodo, get in contact if you have questions!

Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Aug 7

Happy to share the latest from the lab, led by Daniel Alvarez, in collaboration with @lizconibear.bsky.social‬. In this AA-MD tour-de-force, we delve deep into the mechanism and energetics of lipid uptake by bridge-like lipid transfer proteins, and we learn a few interesting things along the way...

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 25

Of course! all trajectories are in Zenodo: doi.org/10.5281/zeno...
If you want more details, just get in touch!

A conserved mechanism of membrane fusion in nuclear pore complex assembly

Molecular dynamics (MD) simulation data for the preprint titled "A conserved mechanism of membrane fusion in nuclear pore complex assembly" are organized into six folders, each named according to the ...

doi.org

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Thanks!!

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Altogether, we think that the mechanism of membrane fusion described in the context of NPC assembly here is different from what known for other fusion machineries (e.g. SNAREs, dynamin-like GTPases,…). More details in the manuscript—let us know your thoughts! (13/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Finally, phylogenetic analyses showed that Brl1/Brr6 homologues are broadly distributed across eukaryotes, and functional experiments in human cells and fly establish CLCC1 as an NPC fusogen in metazoans, consistent with recent preprints by @olzmannlab.bsky.social, Xiao-Wei Chen‬ and others. (12/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

We also modelled Brl1 in curved membranes (a vesicle mimicking the INM shape). Same result: Brl1/Brr6 oligomers stably interacting and promoting lipid mixing within the channel. (11/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

When observed closely, lipid mixing looks like classic hemifusion-like intermediates with exposed lipid-tails (but stabilized within protein rings here). (10/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

But here is another interesting part: interaction between Brl1 and Brr6 only happens when the membranes are < 10 nm apart. This is also very consistent with previous measurement of these distances in NPC assembly intermediates prior to fusion. (9/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

We went back to simulations of opposed bilayers, but with protein oligomers in both of them. We observed a gradual decrease in membrane distances to the point of interaction between proteins (Brl1 and Brr6). This interaction results in lipid mixing in the central channel of the rings. (8/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

This hydrophobic loop motif is highly conserved in fungi, and disrupting this loop halted NPC assembly process. This is telling us that Brl1/Brr6 head-to-head interaction is essential for NPC assembly. (7/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Given that both Brl1 and Brr6 are essential, and their interaction has been studied in earlier work, we modeled 16 copies of Brl1 together with 16 of Brr6. We got a 32-mer complex with two subunits of 16-mers of Brl1/Brr6 with a head-to-head interaction mediated by a hydrophobic loop motif. (6/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Our MD simulations of ring oligomers of Brl1/Brr6 showed pronounced lipid-remodeling in its vicinity. Could this lipid remodeling be enough to drive fusion of INM-ONM? The answer is NO, based on simulation of two opposed bilayers, with protein in only one of them. (5/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

AF3 led us to find that both Brl1 and Brr6 tend to self-associate and form multimeric structures that become fully closed rings when 10 or more copies are present. By mutating charged residues at the dimer interface, we showed that this side-by-side oligomerization is critical. (4/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

We found that Brl1 localizes to NPC assembly sites via an N-terminal nuclear export signal (NES). At that site, Brl1 and Brr6 oligomerize into rings, bridging membranes by interacting through conserved hydrophobic loops, promoting lipid mixing. Continue for more details! (3/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Meet Brl1 and Brr6: two highly conserved transmembrane proteins in yeast, localized to the inner (INM) and outer nuclear membranes (ONM), respectively. Both are essential for NPC assembly, and despite their similarity, they are non-redundant. (2/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 23

Happy to share the latest work from the lab, led by @mudgal17.bsky.social‬, in collaboration with the Weis lab @ethzurich.bsky.social.
How do nuclear membranes fuse during NPC assembly? We answer this question in our latest work, where we identify a new mechanism for membrane fusion… (1/13)

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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · Jul 3

Congratulations Matthieu!!!!

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