Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
| Autor: | Ernesto E. Ambroggio, Bruno Goud, Bruno Antonny, Jean-Baptiste Manneville, James E. Sillibourne |
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| Rok vydání: | 2012 |
| Předmět: |
Biochemistry
Arfaptin2 Substrate Specificity purl.org/becyt/ford/1 [https] Cell membrane Arf1 Molecular Cell Biology 0303 health sciences Liposome Multidisciplinary Tubes Membrane tubulation Chemistry Vesicle 030302 biochemistry & molecular biology GUVs Recombinant Proteins Cellular Structures Transport protein Protein Transport medicine.anatomical_structure Membrane Membrane curvature Medicine Membranes and Sorting Guanosine Triphosphate CIENCIAS NATURALES Y EXACTAS Research Article Otras Ciencias Biológicas Science Materials Science Biophysics Protein Chemistry Ciencias Biológicas Biomaterials 03 medical and health sciences Chemical Biology medicine Humans purl.org/becyt/ford/1.6 [https] Protein Interactions Biology Unilamellar Liposomes 030304 developmental biology Adaptor Proteins Signal Transducing Cell Membrane Proteins Subcellular Organelles Amphiphysin Liposomes ADP-Ribosylation Factor 1 |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 4, p e62963 (2013) CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
| ISSN: | 1932-6203 |
| Popis: | Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation. We report here that active Arf1 is required for the recruitment of Arfaptin2 to artificial liposomes mimicking the Golgi apparatus lipid composition. The Arf1-dependent recruitment of Arfaptin2 increases with membrane curvature, while the recruitment of Arf1 itself is not sensitive to curvature. At high protein concentrations, the binding of Arfaptin2 induces membrane tubulation. Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. These results show that both Arf1 activation and high membrane curvature are required for efficient recruitment of Arfaptin2 to membranes. Fil: Ambroggio, Ernesto Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina Fil: Sillibourne, James. Institute Curie; Francia Fil: Bruno, Antonny. Universite de Nice Sophia Antipolis et CNR; Francia Fil: Manneville, Jean-Baptiste. Institute Curie; Francia Fil: Bruno, Goud. Institute Curie; Francia |
| Databáze: | OpenAIRE |
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