Krishna Mudumbi

@krishnamudumbi.bsky.social

• Assistant Professor at Vanderbilt and the Ingram Cancer Center • Studying membrane protein signaling using single-molecule microscopy • Mentorship and science advocacy in all its forms https://lab.vanderbilt.edu/mudumbi-lab/

Congrats to all the #AQLM2026 participants, especially our very own Isabella Silveltri, for finishing this amazing course! I highly recommend this to anyone interested in learning more about microscopy - these MBL courses are life changing!

Analytical and Quantitative Light Microscopy Course@aqlm.bsky.social · 3mo ago

That’s a wrap on #AQLM 2026 🔬Thank you to everyone who made this year’s course possible: students, faculty, TAs and vendors. We are looking forward to what this #microscopy community builds next. Interested in applying next year? 2027 applications open in late 2026, stay tuned for updates.

I chat with the barista's at Starbucks about our research and they've taken to drawing cell related things on my coffee (one even visited the lab)! I present to you all a cilliated cell on my Frap! Who says science communication can't be fun or tasty?!

A mocha frappuchino with a drawing of a cell on purple

Is PI life modifying a grant proposal as you're finaling last minute things for your brother's wedding in T-minus 16 hours?! Just have to make sure I don't bring up signal transduction in my speech or childhood stupidity in my grant!

I would much rather have early-career researchers like myself have a higher chance to actually get a grant than get a grant that's frontloaded. I likely cannot spend it in a year anyway, unless we can now just buy expensive capital equipment like microscopes and mass specs on them, which I doubt.

Michael D. Green, PhD@michaeldgreen.phd · 5mo ago

Bhattacharya on multi-year funding: “Sometimes for early-career scientists what you need is a front-loaded grant because they’re building their lab and so they can’t wait until year two or three to get the money, so it’s scientifically justified,” When you apply you don’t get to request MYF…

Fellow new PI success PSA! @krishnamudumbi.bsky.social et al have an awesome preprint out! Super psyched to connect with @jasonzxzhang.bsky.social as well, I see collaborations in our future 😀

Krishna Mudumbi@krishnamudumbi.bsky.social · 6mo ago

Not new, but a new to us update: The first preprint out of my lab! We joined forces with @kinasekid.bsky.social @jasonzxzhang.bsky.social and David Baker to study protein phosphorylation! Congrats to Isabella from my lab on her first first author paper! tinyurl.com/43jwwfua

It was such a fun journey working with Krishna’s lab and @kinasekid.bsky.social! Really excited to see where this phospho-binder technology goes!

Krishna Mudumbi@krishnamudumbi.bsky.social · 6mo ago

Not new, but a new to us update: The first preprint out of my lab! We joined forces with @kinasekid.bsky.social @jasonzxzhang.bsky.social and David Baker to study protein phosphorylation! Congrats to Isabella from my lab on her first first author paper! tinyurl.com/43jwwfua

Not new, but a new to us update: The first preprint out of my lab! We joined forces with @kinasekid.bsky.social @jasonzxzhang.bsky.social and David Baker to study protein phosphorylation! Congrats to Isabella from my lab on her first first author paper! tinyurl.com/43jwwfua

De novo design of phosphotyrosine peptide binders

Phosphorylation on tyrosine is a key step in many signaling pathways. Despite recent progress in de novo design of protein binders, there are no current methods for designing binders that recognize phosphorylated proteins and peptides; this is a challenging problem as phosphate groups are highly charged, and phosphorylation often occurs within unstructured regions. Here we introduce RoseTTAFold Diffusion 2 for Molecular Interfaces (RFD2-MI), a deep generative framework for the design of binders for protein, ligand, and covalently modified protein targets. We demonstrate the power and versatility of this method by designing binders for four critical phosphotyrosine sites on three clinically relevant targets: Cluster of Differentiation 3 (CD3ε), Epidermal Growth Factor Receptor (EGFR), Insulin Receptor (INSR) and Signal Transducer and Activator of Transcription 5 (STAT5). Experimental characterization shows that the designs bind their phosphotyrosine containing targets with affinities comparable to native binding sites and have negligible binding to non-phosphorylated targets or phosphopeptides with different sequences. X-ray crystal structures of generated binders to CD3ε and EGFR are very close to the design models, demonstrating the accuracy of the design approach. A designed binder to an EGFR intracellular region phosphorylated upon EGF activation co-localizes with the receptor following EGF stimulation in single-particle tracking (SPT) experiments, demonstrating pY specific recognition in living cells. RFD2-MI provides a generalizable all-atom diffusion framework for probing and modulating phosphorylation-dependent signaling, and more generally, for developing research tools and targeted therapeutics against post-translationally modified proteins. ### Competing Interest Statement The authors have declared no competing interest. NIH NCI, 1K99CA293001

biorxiv.org

Remembering today that having your heart broken is a necessary step on the path to becoming fully human. Whichever heartbreak is your first, it’s probably critical that a state break your heart so that you can develop a political imagination. If this is your first, I’m sorry and also welcome.

A 35 year old letter to the editor, written by a very ballsy 15 year old, about the Rodney King verdict.

What an amazing #CellBio2025! What I took away was that the cell bio community was just as vibrant as ever. Despite the challenges of the past year, I heard so much exciting science and celebrated many accomplishments of my friends and colleagues! Thank you! 🙏🏾

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Excited to host this session on Wednesday with these lovely ladies and some new friends that we made as well! Come check out the amazing talks that were selected!

Chrystal Starbird@drstarbird.bsky.social · 8mo ago

Attending #CellBio2025? Come join the Signaling Squad at our mini symposium on “Spatiotemporal Control of Cell Signaling Across Scales” in Room 120 from 9-11 am! I’m not saying we’re the best because there are so many great sessions, but it may be a save the best for last situation 😉

I found myself fully agreeing with and reflected by this essay and felt that it really hit the mark for me! I find that being my authentic silly self makes me a better scientist and, hopefully, a better mentor (I'll report back on the latter bit in a few more years with more data points)!

Science Magazine@science.org · 9mo ago

"In the end, I have come to realize that being authentic at work is not a weakness, but rather a strength." #ScienceWorkingLife https://scim.ag/49B7hRv

An illustration of a woman wearing an axolotl costume in front of an audience, with text: Embracing my silly side makes me a better scientist. I wish I’d done it sooner