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Membrane targeting of the yeast exocyst complex
R. Pleskot, L. Cwiklik, P. Jungwirth, V. Žárský, M. Potocký,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- buněčná membrána chemie metabolismus MeSH
- exocytóza * MeSH
- fosfatidylinositol-4,5-difosfát chemie metabolismus MeSH
- kinetika MeSH
- mutace MeSH
- podjednotky proteinů chemie genetika metabolismus MeSH
- rho proteiny vázající GTP chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae - proteiny chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae genetika metabolismus MeSH
- sekreční dráha MeSH
- simulace molekulární dynamiky MeSH
- vazba proteinů MeSH
- vezikulární transportní proteiny chemie genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The exocytosis is a process of fusion of secretory vesicles with plasma membrane, which plays a prominent role in many crucial cellular processes, e.g. secretion of neurotransmitters, cytokinesis or yeast budding. Prior to the SNARE-mediated fusion, the initial contact of secretory vesicle with the target membrane is mediated by an evolutionary conserved vesicle tethering protein complex, the exocyst. In all eukaryotic cells, the exocyst is composed of eight subunits - Sec5, Sec6, Sec8, Sec10, Sec15, Exo84 and two membrane-targeting landmark subunits Sec3 and Exo70, which have been described to directly interact with phosphatidylinositol (4,5)-bisphosphate (PIP2) of the plasma membrane. In this work, we utilized coarse-grained molecular dynamics simulations to elucidate structural details of the interaction of yeast Sec3p and Exo70p with lipid bilayers containing PIP2. We found that PIP2 is coordinated by the positively charged pocket of N-terminal part of Sec3p, which folds into unique Pleckstrin homology domain. Conversely, Exo70p interacts with the lipid bilayer by several binding sites distributed along the structure of this exocyst subunit. Moreover, we observed that the interaction of Exo70p with the membrane causes clustering of PIP2 in the adjacent leaflet. We further revealed that PIP2 is required for the correct positioning of small GTPase Rho1p, a direct Sec3p interactor, prior to the formation of the functional Rho1p-exocyst-membrane assembly. Our results show the critical importance of the plasma membrane pool of PIP2 for the exocyst function and suggest that specific interaction with acidic phospholipids represents an ancestral mechanism for the exocyst regulation.
Department of Experimental Plant Biology Charles University Prague 128 44 Prague Czech Republic
Department of Physics Tampere University of Technology FI 33101 Tampere Finland
Citace poskytuje Crossref.org
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- $a Membrane targeting of the yeast exocyst complex / $c R. Pleskot, L. Cwiklik, P. Jungwirth, V. Žárský, M. Potocký,
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- $a The exocytosis is a process of fusion of secretory vesicles with plasma membrane, which plays a prominent role in many crucial cellular processes, e.g. secretion of neurotransmitters, cytokinesis or yeast budding. Prior to the SNARE-mediated fusion, the initial contact of secretory vesicle with the target membrane is mediated by an evolutionary conserved vesicle tethering protein complex, the exocyst. In all eukaryotic cells, the exocyst is composed of eight subunits - Sec5, Sec6, Sec8, Sec10, Sec15, Exo84 and two membrane-targeting landmark subunits Sec3 and Exo70, which have been described to directly interact with phosphatidylinositol (4,5)-bisphosphate (PIP2) of the plasma membrane. In this work, we utilized coarse-grained molecular dynamics simulations to elucidate structural details of the interaction of yeast Sec3p and Exo70p with lipid bilayers containing PIP2. We found that PIP2 is coordinated by the positively charged pocket of N-terminal part of Sec3p, which folds into unique Pleckstrin homology domain. Conversely, Exo70p interacts with the lipid bilayer by several binding sites distributed along the structure of this exocyst subunit. Moreover, we observed that the interaction of Exo70p with the membrane causes clustering of PIP2 in the adjacent leaflet. We further revealed that PIP2 is required for the correct positioning of small GTPase Rho1p, a direct Sec3p interactor, prior to the formation of the functional Rho1p-exocyst-membrane assembly. Our results show the critical importance of the plasma membrane pool of PIP2 for the exocyst function and suggest that specific interaction with acidic phospholipids represents an ancestral mechanism for the exocyst regulation.
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- $a Cwiklik, Lukasz $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague, Czech Republic; J. Heyrovsky Institute of Physical Chemistry, Academy of Sciences of the Czech Republic, 182 23 Prague, Czech Republic.
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- $a Jungwirth, Pavel $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague, Czech Republic; Department of Physics, Tampere University of Technology, FI-33101 Tampere, Finland.
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- $a Žárský, Viktor $u Institute of Experimental Botany, Academy of Sciences of the Czech Republic, 165 02 Prague, Czech Republic; Department of Experimental Plant Biology, Charles University in Prague, 128 44 Prague, Czech Republic.
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- $a Potocký, Martin $u Institute of Experimental Botany, Academy of Sciences of the Czech Republic, 165 02 Prague, Czech Republic. Electronic address: potocky@ueb.cas.cz.
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