Fromme Lab

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

715 followers618 following43 posts

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Fromme Lab
@fromme-lab.bsky.social

Huge kudos to JCB. Not only was the review process super constructive, they enthusiastically embraced the underutilized #GolgiTime hashtag 😀

Journal of Cell Biology@jcb.org

Avl9 defines a family of DENN domain GTPase-activating proteins. New study from Ryan C. Vignogna (@rvig.bsky.social) & J. Christopher Fromme (@fromme-lab.bsky.social) @cornelluniversity.bsky.social: rupress.org/jcb/article/... #GolgiTime #GTPases #Migration #Biochemistry #StructuralBiology #Golgi

Fromme Lab
@fromme-lab.bsky.social

Another important #GolgiTime paper from the Glick lab:

The EMBO Journal@embojournal.org

Kinetic and functional analyses identify the distinct pathways for recycling of resident Golgi proteins regulated by key Golgi-associated tethers Benjamin Glick and coworkers link.springer.com/article/10.1...

link.springer.comGolgi-associated tethers capture vesicles from specific membrane recycling pathways - The EMBO JournalDuring maturation of a Golgi cisterna, a series of vesicular transport pathways recycle resident Golgi proteins. Recycling vesicles are captured by Golgi-associated tethers. Here, we examined three of...

Fromme Lab reposted

Liz Miller
@lizmillercu.bsky.social

*JobAlert* One more week to apply for a post-doc position in my lab at Dundee to study co-translational protein quality control of secretory and membrane proteins. This is a collaborative project with @kulathu.bsky.social and @zeqiraj.bsky.social www.jobs.ac.uk/job/DSM201/p...

jobs.ac.ukPostdoctoral Research Assistant - UOD2336 at University of DundeeDiscover an exciting academic career path as a Postdoctoral Research Assistant - UOD2336 at jobs.ac.uk. Don't miss out on this job opportunity - apply today!

Fromme Lab reposted

Fran Bottanelli
@franbottanelli.bsky.social

It was fun writing this with David @dgershlick.bsky.social! Check it our if you want to hear our view on small #GTPases networks in endosomal trafficking :) part of the themed issue on Membrane trafficking edited by @fromme-lab.bsky.social and Philippe Chavrier www.sciencedirect.com/science/arti...

sciencedirect.comDynamic GTPase networks reshaping endosomal organelle identitiesEndosomal GTPases, while often used as markers for specific endosomal organelles, functionalize the surface of endosomal compartments into biochemical…

Fromme Lab reposted

Ishier Raote
@ishier.bsky.social

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.

Fromme Lab
@fromme-lab.bsky.social

Another fantastic #GolgiTime paper from the Glick lab!

Journal of Cell Biology@jcb.org

Krahn, Glick et al. use budding yeast to examine membrane recycling at the Golgi apparatus. They describe an in vivo vesicle capture assay that reveals which resident Golgi proteins recycle together in the same vesicles. rupress.org/jcb/article/... #Organelles #Trafficking

Fromme Lab reposted

Cohen Lab @Cornell
@cohenlab.bsky.social

Very proud of this tour de force from two former students, Stephanie Tanis and Leah Simon, with help from a huge team, including @charlesdanko.bsky.social highlighting a novel-overlooked intervention point for male contraception www.pnas.org/doi/10.1073/...

pnas.orgMeiotic prophase I disruption as a strategy for nonhormonal male contraception using small-molecule inhibitor JQ1 | PNASDeveloping safe, reversible, and nonhormonal male contraceptives has been hindered by the lack of defined biological windows that can be transientl...

Fromme Lab reposted

brookscrickard1.bsky.social
@brookscrickard1.bsky.social

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...

genesdev.cshlp.orgThe 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

Fromme Lab reposted

David Teis
@teislab.bsky.social

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!

Fromme Lab
@fromme-lab.bsky.social

And here is the working URL! events.faseb.org/event/Small-...

events.faseb.orgHome - Regulation and Function of Small GTPases.Discover the latest in small GTPases research from cell signaling to disease at this global forum for biology, medicine, and therapeutic innovation.
Fromme Lab@fromme-lab.bsky.social

A reminder for all GTPase enthusiasts! The 2026 Regulation and Function of Small GTPases FASEB conference will be held June 21-24 in Florida, USA. The deadline to be considered for a short talk is April 27. events.faseb.org/event/Small-...

Fromme Lab reposted

Jeremy Baskin
@jeremybaskin.bsky.social

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 👇

Fromme Lab
@fromme-lab.bsky.social

Congratulations!

Jeremy Baskin@jeremybaskin.bsky.social

New paper in @jcb.org! We found a new regulator of p62 phase separation, autophagy, and antioxidant signaling. It is an E3 ligase adaptor called SHKBP1, but the effect is via direct p62 binding, not ubiquitination. Congrats to Lin Luan & team! @weillinstitute.bsky.social

Fromme Lab reposted

Brett Collins
@brettcollins.bsky.social

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.

biorxiv.orgThe GTPase activating protein Gyp6 binds Retromer and inactivates Rab7/Ypt7 to coordinate the formation of endosomal carriersThe 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
Fromme Lab
@fromme-lab.bsky.social

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

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 👇

nature.comMembrane editing with proximity labeling reveals regulators of lipid homeostasis - Nature Chemical BiologyCoupling an optogenetic lipid-modifying enzyme with proximity labeling reveals protein networks and mechanisms regulating lipid homeostasis in the membranes of target organelles.
Fromme Lab
@fromme-lab.bsky.social

Awesome opportunity!

Tara Fischer@tarafisch.bsky.social

Perfect time to announce that we are hiring for 1 postdoc and 1 tech to start in the Spring-Summer! If you are excited about organelle quality control, innate immunity, and/or neurodegeneration, join us at Cornell in beautiful Ithaca, NY! More info coming soon fischer.wicmb.cornell.edu pls share 🙏

fischer.wicmb.cornell.eduThe Fischer Lab – Researching fundamental organelle biology in cellular health and disease.
Fromme Lab
@fromme-lab.bsky.social

We are so happy that @tarafisch.bsky.social has joined us at Cornell !!!

Weill Institute for Cell & Molecular Biology@weillinstitute.bsky.social

We are absolutely THRILLED to welcome our newest faculty member @tarafisch.bsky.social to the @weillinstitute.bsky.social community. We look forward to the exciting and impactful work ahead! news.cornell.edu/stories/2026...

news.cornell.eduWeill Institute welcomes Tara Fischer as newest research member | Cornell ChronicleFischer investigates how cells detect and repair organelle damage, and how these processes influence inflammation and the progression of neurodegenerative disease.

Fromme Lab reposted

Weill Institute for Cell & Molecular Biology
@weillinstitute.bsky.social

We are absolutely THRILLED to welcome our newest faculty member @tarafisch.bsky.social to the @weillinstitute.bsky.social community. We look forward to the exciting and impactful work ahead! news.cornell.edu/stories/2026...

news.cornell.eduWeill Institute welcomes Tara Fischer as newest research member | Cornell ChronicleFischer investigates how cells detect and repair organelle damage, and how these processes influence inflammation and the progression of neurodegenerative disease.
Fromme Lab
@fromme-lab.bsky.social

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

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...

biorxiv.orgAvl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functionsRas-related GTPases are molecular switches regulating hundreds of signaling and trafficking pathways in cells. Many GTPase regulators remain to be identified despite extensive genetic and biochemical ...

Fromme Lab reposted

Smolka Lab
@smolka-lab.bsky.social

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

Fromme Lab
@fromme-lab.bsky.social

Sarah and the Cohen lab are doing amazing work!!!

Sarah Cohen@cohenlaboratory.bsky.social

Ithaca is gorge-ous! Thank you @fromme-lab.bsky.social, @jeremybaskin.bsky.social and colleagues for a very fun and stimulating visit to the Weill Institute for Cell and Molecular Biology at Cornell!

Fromme Lab reposted

Jeremy Baskin
@jeremybaskin.bsky.social

Move over, mole day: happy #bioorthogonal copper-free click chemistry day to all who celebrate! 🎉 www.livescience.com/chemistry/sc... @carolynbertozzi.bskyverified.social

livescience.comScience history: Scientists use 'click chemistry' to watch molecules in living organisms — Oct. 23, 2007Carolyn Bertozzi and colleagues laid out a way to make paradigm-shifting "click-chemistry" compatible with living cells, opening up a window into living organisms.

Fromme Lab reposted

Ishier Raote
@ishier.bsky.social

New preprint from Sean Munro @cellbiol-mrclmb.bsky.social! Golgi tether p115 directly binds Sec16A at ER exit sites. Mutations blocking this binding reduce secretion. A rich new mechanistic insight into physical coupling of ERES–ERGIC/Golgi. www.biorxiv.org/content/10.1...

biorxiv.orgThe Golgi vesicle tether p115/USO1 can bind directly to the ER exit site organiser Sec16ANewly-made secretory and membrane proteins exit the endoplasmic reticulum (ER) in COPII vesicles that form at specialised ER exit sites. These exit sites are typically near to the early Golgi compartm...

Fromme Lab reposted

Jeremy Baskin
@jeremybaskin.bsky.social

Thanks to the Cornell Chronicle and @research-and-innovation.cornell.edu for highlighting our new small molecules targeting lipid-binding proteins in cancer! news.cornell.edu/stories/2025...

news.cornell.eduCornell team finds new way to cut cancer’s lipid lifeline | Cornell ChronicleResearchers at Cornell have uncovered molecules that can preserve crucial cellular processes while blocking malignant proteins, indicating a new approach to fighting cancer
Jeremy Baskin@jeremybaskin.bsky.social

A while back we found that the lipid-binding protein PLEKHA4 boosts Wnt/β-catenin signaling and drives melanoma growth in vivo. Now, we (Nathan Frederick) identify small-molecule inhibitors of PLEKHA4 & related proteins with anticancer activity in vitro! pubs.acs.org/doi/10.1021/....

pubs.acs.orgDiscovery, Optimization, and Anticancer Activity of Lipid-Competitive Pleckstrin Homology Domain-Containing Family A InhibitorsPhosphoinositide signaling is a major cellular mechanism controlling cancer cell viability, proliferation, and survival. Yet, inhibition of lipid kinases that produce oncogenic phosphoinositides has afforded only a limited number of efficacious drugs attributed in large part to on-target toxicity resulting from the pleiotropic effects of these signaling lipids. Targeting the specific phosphoinositide effector pathways via competitive inhibitors of phosphoinositide-recognizing pleckstrin homology (PH) domains represents a relatively unexplored means to achieve greater specificity. Herein, we present the discovery from in silico screening, structure–activity relationship (SAR) optimization, and cellular characterization of novel phosphoinositide-competitive inhibitors of the pleckstrin homology domain-containing A (PLEKHA) family. These compounds induce cytotoxic effects in BRAF and NRAS mutant melanoma cells, consistent with on-target inhibition, and the most potent compound is activated by endogenous esterase activity, suggesting that prodrug esters represent a viable strategy for targeting the phosphoinositide-binding pockets of the PLEKHA family of PH domains.

Fromme Lab reposted

Jeremy Baskin
@jeremybaskin.bsky.social

A while back we found that the lipid-binding protein PLEKHA4 boosts Wnt/β-catenin signaling and drives melanoma growth in vivo. Now, we (Nathan Frederick) identify small-molecule inhibitors of PLEKHA4 & related proteins with anticancer activity in vitro! pubs.acs.org/doi/10.1021/....

pubs.acs.orgDiscovery, Optimization, and Anticancer Activity of Lipid-Competitive Pleckstrin Homology Domain-Containing Family A InhibitorsPhosphoinositide signaling is a major cellular mechanism controlling cancer cell viability, proliferation, and survival. Yet, inhibition of lipid kinases that produce oncogenic phosphoinositides has afforded only a limited number of efficacious drugs attributed in large part to on-target toxicity resulting from the pleiotropic effects of these signaling lipids. Targeting the specific phosphoinositide effector pathways via competitive inhibitors of phosphoinositide-recognizing pleckstrin homology (PH) domains represents a relatively unexplored means to achieve greater specificity. Herein, we present the discovery from in silico screening, structure–activity relationship (SAR) optimization, and cellular characterization of novel phosphoinositide-competitive inhibitors of the pleckstrin homology domain-containing A (PLEKHA) family. These compounds induce cytotoxic effects in BRAF and NRAS mutant melanoma cells, consistent with on-target inhibition, and the most potent compound is activated by endogenous esterase activity, suggesting that prodrug esters represent a viable strategy for targeting the phosphoinositide-binding pockets of the PLEKHA family of PH domains.

Fromme Lab reposted

Briggs Group
@briggsgroup.bsky.social

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/...

science.orgThe mechanistic basis of cargo selection during Golgi maturationResident proteins of the Golgi recycle in vesicles and the protein GOLPH3 enables the COPI vesicle coat to accomplish this.

Fromme Lab reposted

Peter Cullen
@peterjcullen1.bsky.social

Latest endosomal publication with @brettcollins.bsky.social: Rebeka Butkovic's beautiful work identifying a new Commander assembly, the RAB32-LRMDA-Commander, and its role in melanosome biogenesis. Reveals molecular mechanism of human oculocutaneous albinism type 7. www.nature.com/articles/s41...

nature.comIdentification of a RAB32-LRMDA-Commander membrane trafficking complex reveals the molecular mechanism of human oculocutaneous albinism type 7Nature Communications - Membrane trafficking is essential for organelle biogenesis. Here, the authors discover an alternative assembly of the Commander trafficking complex and show its role in...

Fromme Lab reposted

brookscrickard1.bsky.social
@brookscrickard1.bsky.social

Just throwing this out there as a significant conceptual advance in the field www.biorxiv.org/content/10.1...

biorxiv.orgThe Eukaryotic homology search complex distorts donor DNA structure to probe for homologyHomologous recombination (HR) is a DNA double-strand break repair pathway that facilitates genetic exchange and protects damaged replication forks during DNA synthesis. As a template-based repair proc...