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Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains
The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how i...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854595/ https://www.ncbi.nlm.nih.gov/pubmed/20300118 http://dx.doi.org/10.1038/embor.2010.28 |
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author | Lenoir, Marc Coskun, Ünal Grzybek, Michal Cao, Xinwang Buschhorn, Sabine B James, Jonathan Simons, Kai Overduin, Michael |
author_facet | Lenoir, Marc Coskun, Ünal Grzybek, Michal Cao, Xinwang Buschhorn, Sabine B James, Jonathan Simons, Kai Overduin, Michael |
author_sort | Lenoir, Marc |
collection | PubMed |
description | The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. Mutations compromising the exposed hydrophobicity of full-length FAPP2 abolish lipid monolayer binding and compression. The trafficking process begins with an electrostatic approach, phosphoinositide sampling and perpendicular penetration. Extensive protein contacts with PtdIns(4)P and neighbouring phospholipids reshape the bilayer and initiate tubulation through a conserved wedge with features shared by diverse protein modules. |
format | Text |
id | pubmed-2854595 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-28545952010-04-27 Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains Lenoir, Marc Coskun, Ünal Grzybek, Michal Cao, Xinwang Buschhorn, Sabine B James, Jonathan Simons, Kai Overduin, Michael EMBO Rep Scientific Reports The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. Mutations compromising the exposed hydrophobicity of full-length FAPP2 abolish lipid monolayer binding and compression. The trafficking process begins with an electrostatic approach, phosphoinositide sampling and perpendicular penetration. Extensive protein contacts with PtdIns(4)P and neighbouring phospholipids reshape the bilayer and initiate tubulation through a conserved wedge with features shared by diverse protein modules. Nature Publishing Group 2010-04 2010-03-19 /pmc/articles/PMC2854595/ /pubmed/20300118 http://dx.doi.org/10.1038/embor.2010.28 Text en Copyright © 2010, European Molecular Biology Organization http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation without specific permission. |
spellingShingle | Scientific Reports Lenoir, Marc Coskun, Ünal Grzybek, Michal Cao, Xinwang Buschhorn, Sabine B James, Jonathan Simons, Kai Overduin, Michael Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title | Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title_full | Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title_fullStr | Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title_full_unstemmed | Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title_short | Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains |
title_sort | structural basis of wedging the golgi membrane by fapp pleckstrin homology domains |
topic | Scientific Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854595/ https://www.ncbi.nlm.nih.gov/pubmed/20300118 http://dx.doi.org/10.1038/embor.2010.28 |
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