An Atomistic Description of Heterotypic Lipid Exchange by Sec14-like Phosphatidylinositol Transfer Proteins.

Authors

Tien Nguyen, Xiao-Ru Chen, Prashant Singh, Savana Green, M Charles Cahill, Joy M Shaffer, Danish Khan, Trivikram Molugu, Ashley Kidwell, Prasanna Iyer, Kiryl Zhaliazka, Sheena D'Arcy, Vytas A Bankaitis, Tatyana I Igumenova

Published in

bioRxiv : the preprint server for biology. Jul 21, 2026. Epub Jul 21, 2026.

Abstract

Lipid transfer proteins (LTPs) are core regulators of the membrane dynamics, lipid signaling and intracellular communication networks that connect every organelle in the eukaryotic cell. ATP-independent lipid exchange reactions are a hallmark activity of these proteins. These remarkable reactions are essential for the important biological functions of LTPs but how lipid exchange is executed is not at all understood. Herein, we focus on phosphatidylinositol transfer proteins (PITPs) of the highly conserved and highly expanded Sec14/CRAL-Trio-like protein superfamily that potentiate phosphatidylinositol-4-phosphate (PtdIns4P) signaling in eukaryotic cells. Using an integrated structural approach, we describe in atomistic detail the lipid exchange reaction of Sec14-like PITPs. The molecular concepts we identify not only yield insights into how these PITPs integrate metabolic activity with PtdIns4P signaling in cells but also provide a framework for interpreting the functional mechanisms of other LTPs of the Sec14/CRAL-Trio superfamily.

PMID:
42539191
Bibliographic data and abstract were imported from PubMed on 01 Aug 2026.

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