M. A. Parson

Structure of Calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A

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.

Spartin-mediated lipid transfer facilitates lipid droplet turnover

This study identifies spartin as a lipid transfer protein essential for lipid droplet turnover via lipophagy, revealing a new lipid transport module in its senescence domain.

ESAT-6 undergoes self-association at phagosomal pH and an ESAT-6 specific nanobody restricts M. tuberculosis growth in macrophages

This study investigates ESAT-6's self-association under acidic conditions and shows an ESAT-6-specific nanobody inhibits M. tuberculosis growth in macrophages.

Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain

This study identifies the helical domain of p110γ as an allosteric regulator of PI3Kγ activity, showing distinct roles in p110γ-p84 and p110γ-p101 complexes through phosphorylation or nanobody binding.

ATP-competitive and allosteric inhibitors induce differential conformational changes at the auto-inhibitory interface of Akt

This study investigates how ATP-competitive and allosteric inhibitors induce different conformational changes in Akt's auto-inhibitory interface across various phosphorylation states.

Oncogenic mutations of PIK3CA lead to increased membrane recruitment driven by reorientation of the ABD, p85 and C-terminus

This study identifies unique regulatory mechanisms by which oncogenic PIK3CA mutations enhance PI3K membrane recruitment and activation through structural reorientations.

Palmitoylation targets the Calcineurin phosphatase to the Phosphatidylinositol 4-kinase complex at the plasma membrane

This study identifies palmitoylation as a mechanism that localizes CNA{beta}1 to the plasma membrane and Golgi, enabling its interaction with the PI4KA complex and regulating PI4P production.

Biochemical insight into novel Rab-GEF activity of the mammalian TRAPPIII complex

This study investigates the GEF activity of TRAPPIII and TRAPPII complexes toward Rab GTPases using biochemical and structural methods, revealing Rab specificity and membrane interaction mechanisms.