Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization
| Autor: | van Galen, Josse, Olrichs, Nick K, Schouten, Arie, Serrano, Ramon L, Nolte-'t Hoen, Esther N M, Eerland, Ruud, Kaloyanova, Dora, Gros, Piet, Helms, J Bernd, LS Veterinaire biochemie, Sub Crystal and Structural Chemistry, Dep Biochemie en Celbiologie, LS Algemeen B&C |
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| Přispěvatelé: | LS Veterinaire biochemie, Sub Crystal and Structural Chemistry, Dep Biochemie en Celbiologie, LS Algemeen B&C |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Phytic Acid Protein Conformation GLIPR-2 Dimer Ordered by external client Lipid Bilayers Molecular Conformation Biophysics Protein–lipid interaction Golgi Apparatus Crystallography X-Ray Phosphatidylinositols Models Biological Biochemistry Cell membrane chemistry.chemical_compound Protein structure Models medicine Humans Lipid bilayer Chromatography Gel Liposome Crystallography Chemistry Crystal structure Cell Membrane Molecular Membrane Proteins Cell Biology Biological Flow Cytometry Lipids GAPR-1 Membrane medicine.anatomical_structure Membrane protein Liposomes Mutation X-Ray Chromatography Gel Dimerization Plasmids |
| Zdroj: | Biochimica et Biophysica Acta, 1818(9), 2175 |
| ISSN: | 0005-2736 0006-3002 |
| DOI: | 10.1016/j.bbamem.2012.04.016 |
| Popis: | Golgi-Associated Plant Pathogenesis-Related protein 1 (GAPR-1) is a mammalian protein that belongs to the superfamily of plant pathogenesis related proteins group 1 (PR-1). GAPR-1 is a peripheral membrane-binding protein that strongly associates with lipid-enriched microdomains at the cytosolic leaflet of Golgi membranes. Little is known about the mechanism of GAPR‐1 interaction with membranes. We previously suggested that dimerization plays a role in the function of GAPR‐1 and here we report that phytic acid (inositol hexakisphosphate) induces dimerization of GAPR‐1 in solution. Elucidation of the crystal structure of GAPR‐1 in the presence of phytic acid revealed that the GAPR‐1 dimer differs from the previously published GAPR‐1 dimer structure. In this structure, one of the monomeric subunits of the crystallographic dimer is rotated by 28.5°. To study the GAPR‐1 dimerization properties, we investigated the interaction with liposomes in a light scattering assay and by flow cytometry. In the presence of negatively charged lipids, GAPR‐1 caused a rapid and stable tethering of liposomes. [D81K]GAPR‐1, a mutant predicted to stabilize the IP6‐induced dimer conformation, also caused tethering of liposomes. [A68K]GAPR‐1 however, a mutant predicted to stabilize the non‐rotated dimer conformation, is capable of binding to liposomes but did not cause liposome tethering. Our combined data suggest that the charge properties of the lipid bilayer can regulate GAPR‐1 dynamics as a potential mechanism to modulate GAPR‐1 function. |
| Databáze: | OpenAIRE |
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