Fromme Lab

@fromme-lab.bsky.social

We study how cells sort important stuff around their insides and to their outsides - Cornell University in beautiful Ithaca, NY https://fromme.wicmb.cornell.edu

On April 19, 1898, Camillo Golgi first described what we now call the Golgi apparatus - a structure so striking and unusual that it took more than 50 years for scientists to accept it wasn’t just an artefact. April 19 is #GolgiDay! Celebrate the cell’s most iconic and best organelle.

Bild

Very exciting that our new paper on the forces exerted by the Rad51-Rad54 homology search complex is now online. This was a collaborative effort with the Wang here at Cornell, and this work performed primarily by a graduate student, Mitch Woodhouse genesdev.cshlp.org/content/earl...

The eukaryotic homology search complex distorts donor DNA structure to probe for homology

A biweekly scientific journal publishing high-quality research in molecular biology and genetics, cancer biology, biochemistry, and related fields

genesdev.cshlp.org

We offer a PostDoc position for a fully funded project on lipid-encoded #lipidtime protein quality-control checkpoints at the Golgi: great collaborators, excellent working & living conditions & benchspace with a view ;) Please share and repost!

Bild

I've been leading a big project at Methods in Enzymology over the past year or so: editing three back-to-back-to-back volumes of articles describing the latest advances in methods for studying lipids and membranes — thank you to the 50 #lipidtime luminaries who contributed the 51 chapters! Details 👇

Bild

Do you want to know more about how Retromer regulates Rab7 activity in yeast? Of course you do. Check out the new collaboration with Andreas Mayer with work led by Catarina Alves and Kevin Chen.

The GTPase activating protein Gyp6 binds Retromer and inactivates Rab7/Ypt7 to coordinate the formation of endosomal carriers

The Retromer coat is conserved in all eukaryotes and is crucial for the correct intracellular sorting of many transmembrane receptors and lysosomal hydrolases. Retromer is an effector of the late endosomal small GTPase RAB7 and is also implicated in its inactivation required for proper endosomal maturation. Here, we explore the role of controlled GTP hydrolysis by the RAB7 ortholog Ypt7 in the formation of Retromer-coated membrane carriers in yeast. Proximity labelling and genetic ablation identify the GTPase Activating Protein (GAP) Gyp6 as a critical regulator of Ypt7 activity in the context or Retromer. Structural studies show that Retromer recruits Gyp6 through its Vps29 subunit, which recognises a specific PL motif and a secondary binding site in the C-terminal domain of Gyp6. This interaction does not occur with other yeast GAPs. Ablation of the Gyp6-Retromer interface or the catalytic activity of Gyp6 leads to the accumulation of tubular structures on endo-lysosomal compartments and to increased association of Ypt7 with Retromer and its cargo Vps10. These results support a model in which Gyp6 controls the switch from Ypt7-dependent Retromer coat assembly and cargo collection to the departure of the carrier through membrane fission and uncoating. ### Competing Interest Statement The authors have declared no competing interest. National Health and Medical Research Council, https://ror.org/011kf5r70, APP2016410 Swiss National Science Foundation, https://ror.org/00yjd3n13, 31003A_179306, 310030_204713, 10.006.083

biorxiv.org

So in awe of our neighbors, another important study from the Baskin lab using such powerfully clever and elegant tools. Feeding-Fishing for the win!

Jeremy Baskin@jeremybaskin.bsky.social · 7mo ago

Thrilled to share our latest study, led by @reikatei.bsky.social, in @natchembio.nature.com! We began by asking a simple question—how do cells know if they have too much of a lipid in a particular membrane, and how do they respond to rectify this imbalance? www.nature.com/articles/s41... More info 👇

Excited to start 2026 out with a new manuscript from our lab, please check out this thread from superstar postdoc @rvig.bsky.social about how he discovered the function of a conserved secretory protein, and how this also led him to the identification of a new family of GAP proteins!

Ryan Vignogna@rvig.bsky.social · 7mo ago

Mind the GAP 🚧🕳️🚧 Excited to share the latest preprint from the Fromme Lab (@fromme-lab.bsky.social), showing that the DENN domain protein Avl9 functions as an Arf-GAP, revising long-standing assumptions about DENN protein function, 🧵: www.biorxiv.org/content/10.6...

Check out our new biosensor technology to study DDR kinase signaling: ProKAS. We combine: -proteomics -engineered peptide sensors -a new concept of amino acid barcodes ProKAS tracks kinase signaling with spatial resolution and produces highly quantitative data. Just published today: rdcu.be/ePNo0

BildBild