Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.

The formation of vesicles is essential for many biological processes, in particular for the trafficking of membrane proteins within cells. The Endosomal Sorting Complex Required for Transport (ESCRT) directs membrane budding away from the cytosol. Unlike other vesicle formation pathways, the ESCRT-m...

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Autores principales: Bartosz Różycki, Evzen Boura, James H Hurley, Gerhard Hummer
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Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2012
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Acceso en línea:https://doaj.org/article/05e2bb677dd04a869573878b655422b9
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spelling oai:doaj.org-article:05e2bb677dd04a869573878b655422b92021-11-18T05:52:46ZMembrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.1553-734X1553-735810.1371/journal.pcbi.1002736https://doaj.org/article/05e2bb677dd04a869573878b655422b92012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23093927/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358The formation of vesicles is essential for many biological processes, in particular for the trafficking of membrane proteins within cells. The Endosomal Sorting Complex Required for Transport (ESCRT) directs membrane budding away from the cytosol. Unlike other vesicle formation pathways, the ESCRT-mediated budding occurs without a protein coat. Here, we propose a minimal model of ESCRT-induced vesicle budding. Our model is based on recent experimental observations from direct fluorescence microscopy imaging that show ESCRT proteins colocalized only in the neck region of membrane buds. The model, cast in the framework of membrane elasticity theory, reproduces the experimentally observed vesicle morphologies with physically meaningful parameters. In this parameter range, the minimum energy configurations of the membrane are coatless buds with ESCRTs localized in the bud neck, consistent with experiment. The minimum energy configurations agree with those seen in the fluorescence images, with respect to both bud shapes and ESCRT protein localization. On the basis of our model, we identify distinct mechanistic pathways for the ESCRT-mediated budding process. The bud size is determined by membrane material parameters, explaining the narrow yet different bud size distributions in vitro and in vivo. Our membrane elasticity model thus sheds light on the energetics and possible mechanisms of ESCRT-induced membrane budding.Bartosz RóżyckiEvzen BouraJames H HurleyGerhard HummerPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 8, Iss 10, p e1002736 (2012)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Bartosz Różycki
Evzen Boura
James H Hurley
Gerhard Hummer
Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
description The formation of vesicles is essential for many biological processes, in particular for the trafficking of membrane proteins within cells. The Endosomal Sorting Complex Required for Transport (ESCRT) directs membrane budding away from the cytosol. Unlike other vesicle formation pathways, the ESCRT-mediated budding occurs without a protein coat. Here, we propose a minimal model of ESCRT-induced vesicle budding. Our model is based on recent experimental observations from direct fluorescence microscopy imaging that show ESCRT proteins colocalized only in the neck region of membrane buds. The model, cast in the framework of membrane elasticity theory, reproduces the experimentally observed vesicle morphologies with physically meaningful parameters. In this parameter range, the minimum energy configurations of the membrane are coatless buds with ESCRTs localized in the bud neck, consistent with experiment. The minimum energy configurations agree with those seen in the fluorescence images, with respect to both bud shapes and ESCRT protein localization. On the basis of our model, we identify distinct mechanistic pathways for the ESCRT-mediated budding process. The bud size is determined by membrane material parameters, explaining the narrow yet different bud size distributions in vitro and in vivo. Our membrane elasticity model thus sheds light on the energetics and possible mechanisms of ESCRT-induced membrane budding.
format article
author Bartosz Różycki
Evzen Boura
James H Hurley
Gerhard Hummer
author_facet Bartosz Różycki
Evzen Boura
James H Hurley
Gerhard Hummer
author_sort Bartosz Różycki
title Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
title_short Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
title_full Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
title_fullStr Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
title_full_unstemmed Membrane-elasticity model of Coatless vesicle budding induced by ESCRT complexes.
title_sort membrane-elasticity model of coatless vesicle budding induced by escrt complexes.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/05e2bb677dd04a869573878b655422b9
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AT evzenboura membraneelasticitymodelofcoatlessvesiclebuddinginducedbyescrtcomplexes
AT jameshhurley membraneelasticitymodelofcoatlessvesiclebuddinginducedbyescrtcomplexes
AT gerhardhummer membraneelasticitymodelofcoatlessvesiclebuddinginducedbyescrtcomplexes
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