Alexandria L Shaw

This study identifies phosphorylation of Y2090 in PI4KA as an inhibitory mechanism that suppresses its lipid kinase activity through conformational changes and reduced membrane recruitment.

The paper develops a nanobody that selectively blocks EFR3 recruitment of PI4KA by targeting TTC7B, reducing membrane recruitment and PI4P production.

The paper reports a cryo-EM structure of EFR3A bound to the PI4KA complex, revealing the molecular mechanism of PI4KA membrane recruitment and its regulation in human disease.

The paper reports a cryo-EM structure of Calcineurin bound to PI4KA, revealing direct interactions with both PI4KA and FAM126A and their conserved binding sequences.