Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities

Mintu Chandra, Yanni K.-Y. Chin, Caroline Mas, J. Ryan Feathers, Blessy Paul, Sanchari Datta, Kai-En Chen, Xinying Jia, Zhe Yang, Suzanne J. Norwood, Biswaranjan Mohanty, Andrea Bugarcic, Rohan D. Teasdale, W. Mike Henne, Mehdi Mobli and Brett M. Collins ()
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Mintu Chandra: The University of Queensland
Yanni K.-Y. Chin: The University of Queensland
Caroline Mas: The University of Queensland
J. Ryan Feathers: University of Texas Southwestern Medical Center
Blessy Paul: The University of Queensland
Sanchari Datta: University of Texas Southwestern Medical Center
Kai-En Chen: The University of Queensland
Xinying Jia: The University of Queensland
Zhe Yang: The University of Queensland
Suzanne J. Norwood: The University of Queensland
Biswaranjan Mohanty: Monash University
Andrea Bugarcic: The University of Queensland
Rohan D. Teasdale: The University of Queensland
W. Mike Henne: University of Texas Southwestern Medical Center
Mehdi Mobli: The University of Queensland
Brett M. Collins: The University of Queensland

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family.

Date: 2019
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DOI: 10.1038/s41467-019-09355-y

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