👊🧊 I say to my trainees while I teach them about proper grid freezing and handling techniques at the microscope this afternoon.

Structural basis for dimerization, catalytic regulation, and substrate selectivity in S9D proteases www.biorxiv.org/content/10.64898/2026.01.21.700880v1 #cryoEM

Young Alum of the Month: Jacqueline Ehrlich

Loyal forever true ❤️💛 big thanks to career services at ISU CALS for the feature! career.cals.iastate.edu/news/2025/yo...

Happy Halloween from the Kawate lab! Lanes of my *oriole* gel from left to right: ladder, Pannexin 1, MSP2N2, and reconstituted Pannexin1 in MSP2N2 nanodiscs 🤓

Steric repulsion counteracts ER–to–lipid droplet protein movement Steric hindrance affects the relocation of ER-to-LD proteins and primarily regulates the LD proteome.

Two new papers from our lab 😀!
Seipin beyond LDs: balances ER sphingolipids & glycerolipids, key for protein secretion (incl. Cav1). www.cell.com/cell-reports...
ER→LD traffic: lateral steric repulsion shapes how monotopic ER proteins partition onto LDs. www.science.org/doi/10.1126/...

Molecular basis for the regulation of membrane proteins through preferential lipid solvation - Nature Chemical Biology Static protein structures can capture the association of lipids, but it is unclear whether the association is due to lipids acting as long-lived ligands or the solvation of preferred lipids around the protein. A computational-experimental framework has now shown that for the protein CLC-ec1, it is the change in lipid solvation energies that drives dimerization, with preferred lipids around the protein modulating this driving force.

Are the lipids associated with static protein structures there as long-lived ligands or an effect of preferential solvation? This computational-experimental framework shows the way! #lipidtime #compchem

www.nature.com/articles/s41...

POV: you venture over to the #celegans side of the lab @kcrow11.bsky.social

This and yap

This week, I was invited as the Alumni speaker for the Stupka Undergraduate Research Symposium in BBMB at Iowa State University. Sharing my research with my alma mater was a true honor, a highlight of graduate school, and definitely a full circle moment. I am so lucky!

I needed my column to continue washing while I was in lab meeting so I grabbed one of those pesky slow columns et voilà! She’s an innovator today 🤭

Celebrating #internationalwomensday and #womenshistorymonth with this inspiring little read. Bookmarking it with the leather tab made by one of my favorite women, my mom.

Post #bps2025 checklist:
laundry ✅
purify proteins ✅
tell literally everyone how inspired & motivated u are since coming back from LA … ✅

@kcrow11.bsky.social

This is so kind! Thank you so much!! I’m glad you enjoyed it 😌

Had such an amazing time at my first BPS conference! Looking forward to BPS 2026 already!

#bps2025

@jacquelineehrlich.bsky.social @saketbagde.bsky.social @biophysicalsoc.bsky.social

@kcrow11.bsky.social

Kawate Lab 🛫 Los Angeles!! Catch us in a platform session at 4:45 on Tuesday and at the 10:30 poster session on Wednesday #BPS2025

Multitaskin’ this morning

Thank you 🫶🫶

This study puts forth a mechanism by which c-terminal cleavage liberates the CAD causing the repositioning of the N terminus to promote Panx1 channel opening.

We analyzed the electrostatic free energy of the cytosolic NTD, finding a positively charged region inside the pore that could accumulate negatively charged anions like ATP. In the reoriented NTD conformation this negative region is diminished reducing accumulation of ions there.

Our structural studies revealed that when exposed, the cytoplasmic domain, dubbed the c-terminal activating domain (CAD) can compete with the N-terminus to occupy a cytosolic pocket, which forces the N-terminus to reorient into the pore.

In this study, we identified a structure cytoplasmic domain immediately before a caspase cleave site, critical for Panx1 channel opening. This region must be exposed for ion permeation, but if this region is truncated, the channel cannot respond to any opening stimulus.

Joining the @bsky.app party just in time to share my 1st cryo-EM structures from our latest Panx1 story in @pnas.org! I’m so grateful for Cornell’s cryo-EM community (esp @fromme-lab.bsky.social @cryomariena.bsky.social @10feng.bsky.social) in helping us establish cryoEM in our lab the last 5 years!

In this study, we identified a structure cytoplasmic domain immediately before a caspase cleave site, critical for Panx1 channel opening. This region must be exposed for ion permeation, but if this region is truncated, the channel cannot respond to any opening stimulus.