Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10316/10371 https://doi.org/10.1021/bi0024299 |
Resumo: | The role and mechanism of formation of lipid domains in a functional membrane have generally received limited attention. Our approach, based on the hypothesis that thermodynamic coupling between lipid−lipid and protein−lipid interactions can lead to domain formation, uses a combination of an experimental lipid bilayer model system and Monte Carlo computer simulations of a simple model of that system. The experimental system is a fluid bilayer composed of a binary mixture of phosphatidylcholine (PC) and phosphatidylserine (PS), containing 4% of a pyrene-labeled anionic phospholipid. Addition of the C2 protein motif (a structural domain found in proteins implicated in eukaryotic signal transduction and cellular trafficking processes) to the bilayer first increases and then decreases the excimer/monomer ratio of the pyrene fluorescence. We interpret this to mean that protein binding induces anionic lipid domain formation until the anionic lipid becomes saturated with protein. Monte Carlo simulations were performed on a lattice representing the lipid bilayer to which proteins were added. The important parameters are an unlike lipid−lipid interaction term and an experimentally derived preferential protein−lipid interaction term. The simulations support the experimental conclusion and indicate the existence of a maximum in PS domain size as a function of protein concentration. Thus, lipid−protein coupling is a possible mechanism for both lipid and protein clustering on a fluid bilayer. Such domains could be precursors of larger lipid−protein clusters (‘rafts'), which could be important in various biological processes such as signal transduction at the level of the cell membrane. |
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Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein MotifThe role and mechanism of formation of lipid domains in a functional membrane have generally received limited attention. Our approach, based on the hypothesis that thermodynamic coupling between lipid−lipid and protein−lipid interactions can lead to domain formation, uses a combination of an experimental lipid bilayer model system and Monte Carlo computer simulations of a simple model of that system. The experimental system is a fluid bilayer composed of a binary mixture of phosphatidylcholine (PC) and phosphatidylserine (PS), containing 4% of a pyrene-labeled anionic phospholipid. Addition of the C2 protein motif (a structural domain found in proteins implicated in eukaryotic signal transduction and cellular trafficking processes) to the bilayer first increases and then decreases the excimer/monomer ratio of the pyrene fluorescence. We interpret this to mean that protein binding induces anionic lipid domain formation until the anionic lipid becomes saturated with protein. Monte Carlo simulations were performed on a lattice representing the lipid bilayer to which proteins were added. The important parameters are an unlike lipid−lipid interaction term and an experimentally derived preferential protein−lipid interaction term. The simulations support the experimental conclusion and indicate the existence of a maximum in PS domain size as a function of protein concentration. Thus, lipid−protein coupling is a possible mechanism for both lipid and protein clustering on a fluid bilayer. Such domains could be precursors of larger lipid−protein clusters (‘rafts'), which could be important in various biological processes such as signal transduction at the level of the cell membrane.American Chemical Society2001-04-03info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/10371http://hdl.handle.net/10316/10371https://doi.org/10.1021/bi0024299engBiochemistry. 40:13 (2001) 4181-41910006-2960Hinderliter, AnneAlmeida, Paulo F. F.Creutz, Carl E.Biltonen, Rodney L.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2020-05-25T13:13:27Zoai:estudogeral.uc.pt:10316/10371Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:01:14.828596Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
title |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
spellingShingle |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif Hinderliter, Anne |
title_short |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
title_full |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
title_fullStr |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
title_full_unstemmed |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
title_sort |
Domain Formation in a Fluid Mixed Lipid Bilayer Modulated through Binding of the C2 Protein Motif |
author |
Hinderliter, Anne |
author_facet |
Hinderliter, Anne Almeida, Paulo F. F. Creutz, Carl E. Biltonen, Rodney L. |
author_role |
author |
author2 |
Almeida, Paulo F. F. Creutz, Carl E. Biltonen, Rodney L. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Hinderliter, Anne Almeida, Paulo F. F. Creutz, Carl E. Biltonen, Rodney L. |
description |
The role and mechanism of formation of lipid domains in a functional membrane have generally received limited attention. Our approach, based on the hypothesis that thermodynamic coupling between lipid−lipid and protein−lipid interactions can lead to domain formation, uses a combination of an experimental lipid bilayer model system and Monte Carlo computer simulations of a simple model of that system. The experimental system is a fluid bilayer composed of a binary mixture of phosphatidylcholine (PC) and phosphatidylserine (PS), containing 4% of a pyrene-labeled anionic phospholipid. Addition of the C2 protein motif (a structural domain found in proteins implicated in eukaryotic signal transduction and cellular trafficking processes) to the bilayer first increases and then decreases the excimer/monomer ratio of the pyrene fluorescence. We interpret this to mean that protein binding induces anionic lipid domain formation until the anionic lipid becomes saturated with protein. Monte Carlo simulations were performed on a lattice representing the lipid bilayer to which proteins were added. The important parameters are an unlike lipid−lipid interaction term and an experimentally derived preferential protein−lipid interaction term. The simulations support the experimental conclusion and indicate the existence of a maximum in PS domain size as a function of protein concentration. Thus, lipid−protein coupling is a possible mechanism for both lipid and protein clustering on a fluid bilayer. Such domains could be precursors of larger lipid−protein clusters (‘rafts'), which could be important in various biological processes such as signal transduction at the level of the cell membrane. |
publishDate |
2001 |
dc.date.none.fl_str_mv |
2001-04-03 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10316/10371 http://hdl.handle.net/10316/10371 https://doi.org/10.1021/bi0024299 |
url |
http://hdl.handle.net/10316/10371 https://doi.org/10.1021/bi0024299 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochemistry. 40:13 (2001) 4181-4191 0006-2960 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133904780656640 |