Dimerization of the pulmonary surfactant protein C in a membrane environment

Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the st...

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Detalles Bibliográficos
Autores: Korolainen, Hanna, Lolicato, Fabio, Enkavi, Giray, Pérez Gil, Jesús, Kulig, Waldemar, Vattulainen, Ilpo
Tipo de recurso: artículo
Fecha de publicación:2022
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/71853
Acceso en línea:https://hdl.handle.net/20.500.14352/71853
Access Level:acceso abierto
Palabra clave:577.112
Pulmonary surfactant protein C
Dimerization
Bioquímica (Biología)
2302 Bioquímica
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oai_identifier_str oai:docta.ucm.es:20.500.14352/71853
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repository_id_str
spelling Dimerization of the pulmonary surfactant protein C in a membrane environmentKorolainen, HannaLolicato, FabioEnkavi, GirayPérez Gil, JesúsKulig, WaldemarVattulainen, Ilpo577.112Pulmonary surfactant protein CDimerizationBioquímica (Biología)2302 BioquímicaSurfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the structures of functional SP-C complexes have remained unclear. SP-C is known to exist as a primarily α-helical structure with an apparently unstructured N-terminal region, yet there is recent evidence that the functions of SP-C could be associated with the formation of SP-C dimers and higher oligomers. In this work, we used molecular dynamics simulations, two-dimensional umbrella sampling, and well-tempered metadynamics to study the details of SP-C dimerization. The results suggest that SP-C dimerizes in pulmonary surfactant membranes, forming dimers of different topologies. The simulations identified a dimerization motif region V21xxxVxxxGxxxM33 that is much larger than the putative A30xxxG34 motif that is commonly assumed to control the dimerization of some α-helical transmembrane domains. The results provide a stronger basis for elucidating how SP-C functions in concert with other surfactant proteins.Public Library ScienceUniversidad Complutense de Madrid20222022-04-2720222022-04-27journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/71853reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 3.0 Españahttps://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/718532026-06-02T12:44:21Z
dc.title.none.fl_str_mv Dimerization of the pulmonary surfactant protein C in a membrane environment
title Dimerization of the pulmonary surfactant protein C in a membrane environment
spellingShingle Dimerization of the pulmonary surfactant protein C in a membrane environment
Korolainen, Hanna
577.112
Pulmonary surfactant protein C
Dimerization
Bioquímica (Biología)
2302 Bioquímica
title_short Dimerization of the pulmonary surfactant protein C in a membrane environment
title_full Dimerization of the pulmonary surfactant protein C in a membrane environment
title_fullStr Dimerization of the pulmonary surfactant protein C in a membrane environment
title_full_unstemmed Dimerization of the pulmonary surfactant protein C in a membrane environment
title_sort Dimerization of the pulmonary surfactant protein C in a membrane environment
dc.creator.none.fl_str_mv Korolainen, Hanna
Lolicato, Fabio
Enkavi, Giray
Pérez Gil, Jesús
Kulig, Waldemar
Vattulainen, Ilpo
author Korolainen, Hanna
author_facet Korolainen, Hanna
Lolicato, Fabio
Enkavi, Giray
Pérez Gil, Jesús
Kulig, Waldemar
Vattulainen, Ilpo
author_role author
author2 Lolicato, Fabio
Enkavi, Giray
Pérez Gil, Jesús
Kulig, Waldemar
Vattulainen, Ilpo
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.112
Pulmonary surfactant protein C
Dimerization
Bioquímica (Biología)
2302 Bioquímica
topic 577.112
Pulmonary surfactant protein C
Dimerization
Bioquímica (Biología)
2302 Bioquímica
description Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the structures of functional SP-C complexes have remained unclear. SP-C is known to exist as a primarily α-helical structure with an apparently unstructured N-terminal region, yet there is recent evidence that the functions of SP-C could be associated with the formation of SP-C dimers and higher oligomers. In this work, we used molecular dynamics simulations, two-dimensional umbrella sampling, and well-tempered metadynamics to study the details of SP-C dimerization. The results suggest that SP-C dimerizes in pulmonary surfactant membranes, forming dimers of different topologies. The simulations identified a dimerization motif region V21xxxVxxxGxxxM33 that is much larger than the putative A30xxxG34 motif that is commonly assumed to control the dimerization of some α-helical transmembrane domains. The results provide a stronger basis for elucidating how SP-C functions in concert with other surfactant proteins.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022-04-27
2022
2022-04-27
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/71853
url https://hdl.handle.net/20.500.14352/71853
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library Science
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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