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Fromme Lab

@fromme-lab

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

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13.11.2024
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Latest posts by Fromme Lab @fromme-lab

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10.02.2026 18:34 πŸ‘ 2 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

Congratulations!

06.02.2026 20:32 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

Love it

06.02.2026 20:28 πŸ‘ 2 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

Thank you, Alex!!! It was fun watching @rvig.bsky.social solve this puzzle

06.02.2026 15:08 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0
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

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.

28.01.2026 01:25 πŸ‘ 20 πŸ” 10 πŸ’¬ 0 πŸ“Œ 0

Weill Institute is recruiting postdocs, please share!

Fischer Lab: lnkd.in/eMnveqyv

Hu Lab: lnkd.in/epsGK7wd

22.01.2026 17:56 πŸ‘ 4 πŸ” 6 πŸ’¬ 0 πŸ“Œ 0
Conference flyer listing confirmed speakers and attendees

Conference flyer listing confirmed speakers and attendees

Calling all GTPase enthusiasts! The 2026 Regulation and Function of Small GTPases FASEB conference will be held June 22-24 in Florida, USA.

events.faseb.org/event/Small-...

14.01.2026 15:23 πŸ‘ 4 πŸ” 4 πŸ’¬ 0 πŸ“Œ 0

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!

07.01.2026 15:28 πŸ‘ 6 πŸ” 3 πŸ’¬ 0 πŸ“Œ 0

Awesome opportunity!

07.01.2026 15:02 πŸ‘ 2 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

Thank you, Lydia!

06.01.2026 21:25 πŸ‘ 0 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

Thank you, Fran! The Arfs are so powerful they need more regulators πŸ˜€

06.01.2026 20:32 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

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

06.01.2026 18:46 πŸ‘ 3 πŸ” 1 πŸ’¬ 1 πŸ“Œ 0
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Weill Institute welcomes Tara Fischer as newest research member | Cornell Chronicle Fischer investigates how cells detect and repair organelle damage, and how these processes influence inflammation and the progression of neurodegenerative disease.

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...

06.01.2026 18:25 πŸ‘ 21 πŸ” 8 πŸ’¬ 0 πŸ“Œ 2

Thank you, Jeremy!

06.01.2026 18:41 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0

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!

06.01.2026 15:54 πŸ‘ 17 πŸ” 6 πŸ’¬ 2 πŸ“Œ 0

Thank you, Brett!!

06.01.2026 15:48 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0
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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

13.11.2025 18:22 πŸ‘ 20 πŸ” 7 πŸ’¬ 2 πŸ“Œ 1

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

10.11.2025 23:19 πŸ‘ 6 πŸ” 0 πŸ’¬ 1 πŸ“Œ 0
Scaling back DEI programmes and the loss of scientific talent - Nature Cell Biology Programmes that support diversity, equity and inclusion (DEI) in science are under attack in the USA. Data indicate that diversity in the scientific workforce increases creativity and success in tackl...

Important article from @marymunson4.bsky.social @joann-trejo.bsky.social @needhibhalla.bsky.social

29.10.2025 23:26 πŸ‘ 9 πŸ” 9 πŸ’¬ 0 πŸ“Œ 0
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πŸŽ‰ Huge congrats to Maya Schuldiner from the Weizmann Institute (Israel) for the πŸ… Otto Warburg Medal 2026!
Her work on how proteins find their way to organelles and how these organelles talk to each other has reshaped how we think about cells 🧬✨
#OWM #WeizmannInstitute @elsevierconnect.bsky.social

27.10.2025 09:28 πŸ‘ 55 πŸ” 17 πŸ’¬ 0 πŸ“Œ 3
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Science history: Scientists use 'click chemistry' to watch molecules in living organisms β€” Oct. 23, 2007 Carolyn Bertozzi and colleagues laid out a way to make paradigm-shifting "click-chemistry" compatible with living cells, opening up a window into living organisms.

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

23.10.2025 18:34 πŸ‘ 49 πŸ” 6 πŸ’¬ 0 πŸ“Œ 0
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The Golgi vesicle tether p115/USO1 can bind directly to the ER exit site organiser Sec16A Newly-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...

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...

17.10.2025 07:36 πŸ‘ 14 πŸ” 4 πŸ’¬ 0 πŸ“Œ 0

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...

17.10.2025 19:32 πŸ‘ 40 πŸ” 9 πŸ’¬ 2 πŸ“Œ 1
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Postdoctoral Research Assistant - MCDB - UOD2016 Closing date: Thursday 6 November 2025, 23:59

Attention membrane traffickers! I'm recruiting a post-doc to my lab in Dundee. We're dissecting the functions of intrinsically disordered domains of COPII coat proteins. We think they control timing of coat assembly and morphology of carriers.

www.dundee.ac.uk/work-for-us/...

15.10.2025 12:53 πŸ‘ 39 πŸ” 36 πŸ’¬ 0 πŸ“Œ 3
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Discovery, Optimization, and Anticancer Activity of Lipid-Competitive Pleckstrin Homology Domain-Containing Family A Inhibitors Phosphoinositide 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.

A while back we found that the lipid-binding protein PLEKHA4 boosts Wnt/Ξ²-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/....

07.10.2025 16:06 πŸ‘ 26 πŸ” 9 πŸ’¬ 0 πŸ“Œ 2
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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/...

06.10.2025 11:39 πŸ‘ 54 πŸ” 22 πŸ’¬ 0 πŸ“Œ 1
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How do cells sense & respond to lipid imbalances? What happens when a disease-relevant enzyme is blocked? Shiying Huang investigates phosphoinositide lipids with the Balla lab & discovers an integrated cellular response that boosts alternate lipid synthesis pathways! www.biorxiv.org/content/10.1...

03.10.2025 13:03 πŸ‘ 33 πŸ” 12 πŸ’¬ 0 πŸ“Œ 1

Phosphatidylserine and RhoB connect phosphatidylinositol 4-phosphate and phosphatidic acid metabolism at the plasma membrane https://www.biorxiv.org/content/10.1101/2025.09.30.679611v1

02.10.2025 23:30 πŸ‘ 0 πŸ” 1 πŸ’¬ 0 πŸ“Œ 0
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Identification of a RAB32-LRMDA-Commander membrane trafficking complex reveals the molecular mechanism of human oculocutaneous albinism type 7 Nature 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...

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...

02.10.2025 10:30 πŸ‘ 14 πŸ” 5 πŸ’¬ 0 πŸ“Œ 0
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Tenure Track Faculty - Molecular Biology and Genetics - Ithaca, New York job with Cornell University | 675236 Tenure Track Faculty, Molecular Biology and Genetics Weill Institute for Cell and Molecular Biology Department of Molecular Biology and Genetics Co...

We are hiring, come be our colleague!

jobs.sciencecareers.org/job/675236/t...

29.09.2025 14:57 πŸ‘ 1 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0