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Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities
- Source :
- Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019), Nature Communications
- Publication Year :
- 2019
- Publisher :
- Nature Publishing Group, 2019.
-
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.<br />Phox homology (PX) domains are membrane interacting domains that bind to various lipids. Here authors screen all human PX domains systematically for their phospholipid preferences and define four classes and provide the basis for defining and predicting functional PX-membrane interactions.
- Subjects :
- Models, Molecular
0301 basic medicine
Protein family
Science
Endocytic cycle
General Physics and Astronomy
02 engineering and technology
Calorimetry
Phosphatidylinositols
Article
General Biochemistry, Genetics and Molecular Biology
Homology (biology)
03 medical and health sciences
Protein Domains
Sequence Analysis, Protein
Organelle
Humans
Binding site
lcsh:Science
Sorting Nexins
Binding Sites
Multidisciplinary
Chemistry
Isothermal titration calorimetry
General Chemistry
PX domain
021001 nanoscience & nanotechnology
3. Good health
Transport protein
Interferometry
030104 developmental biology
Biochemistry
lcsh:Q
0210 nano-technology
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 10
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....8e80d373bbebc6f6531cec7673bd7860