I’m deeply grateful to everyone involved in this work, and especially to my great friend and supervisor @irenemangialavori.bsky.social for her guidance and support throughout this project. (4/4)
In some lipid environments, inhibition is strong; in others, it is reduced or even reversed.
These findings highlight how membrane composition can fine-tune the regulation of a critical calcium pump and the importance of protein–lipid interactions in controlling membrane protein function. (3/4)
We explored how the lipid environment surrounding PMCA modulates its inhibition by aluminum. Using biophysical approaches including small-angle X-ray scattering, fluorescence probes, and activity assays, we found that aluminum’s impact on PMCA is highly dependent on membrane context. (2/4)
I’m excited to share another publication from my PhD:
authors.elsevier.com/a/1meGTWFfh2...
The plasma membrane Ca²⁺-ATPase (PMCA) is a key enzyme responsible for maintaining intracellular calcium homeostasis by actively extruding Ca²⁺ from the cell. (1/4)
Dissociated VP7 monomers form a single, large, cooperative pore, seen both in cells and in liposomes. An amphipathic VP7 helix is sufficient for perforation, enabling rapid DLP release and immediate viral transcription in the cytosol (3/3).
We show that entry is a two-step membrane insertion process. VP4 spikes switch from upright (attachment) to reversed (insertion of foot domain). This triggers Ca²⁺ leakage from vesicle, Ca2+ signaling and ultimately VP7 dissociation (2/3)
Check out our new preprint! We uncover the full molecular mechanism of rotavirus membrane penetration and cytosolic escape using cryo-ET, live-cell imaging, and single-molecule assays. (1/3)
🔗 biorxiv.org/content/10.6...
