A cholesterol recognition motif in human phospholipid scramblase 1

Autores
Posada, Itziar M. D.; Fantini, Jacques; Contreras, F. Xabier; Barrantes, Francisco Jose; Alonso, Alicia; Goñi, Félix M.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Human phospholipid scramblase 1 (SCR) catalyzes phospholipid transmembrane (flip-flop) motion. This protein is assumed to bind the membrane hydrophobic core through a transmembrane domain (TMD) as well as via covalently bound palmitoyl residues. Here, we explore the possible interaction of the SCR TMD with cholesterol by using a variety of experimental and computational biophysical approaches. Our findings indicate that SCR contains an amino acid segment at the C-terminal region that shows a remarkable affinity for cholesterol, although it lacks the CRAC sequence. Other 3-OH sterols, but not steroids lacking the 3-OH group, also bind this region of the protein. The newly identified cholesterol-binding region is located partly at the C-terminal portion of the TMD and partly in the first amino acid residues in the SCR C-terminal extracellular coil. This finding could be related to the previously described affinity of SCR for cholesterol-rich domains in membranes.
Fil: Posada, Itziar M. D.. Universidad del País Vasco; España
Fil: Fantini, Jacques. Universidad de Aix-Marsella; Francia
Fil: Contreras, F. Xabier. Universidad del País Vasco; España. Ikerbasque; España
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas; Argentina
Fil: Alonso, Alicia. Universidad del País Vasco; España
Fil: Goñi, Félix M.. Universidad del País Vasco; España
Materia
MEMBRANE PROTEIN
CHOLESTEROL
PROTEIN-LIPID INTERACTIONS
ENZYME
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/98814
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/98814
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A cholesterol recognition motif in human phospholipid scramblase 1Posada, Itziar M. D.Fantini, JacquesContreras, F. XabierBarrantes, Francisco JoseAlonso, AliciaGoñi, Félix M.MEMBRANE PROTEINCHOLESTEROLPROTEIN-LIPID INTERACTIONSENZYMEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Human phospholipid scramblase 1 (SCR) catalyzes phospholipid transmembrane (flip-flop) motion. This protein is assumed to bind the membrane hydrophobic core through a transmembrane domain (TMD) as well as via covalently bound palmitoyl residues. Here, we explore the possible interaction of the SCR TMD with cholesterol by using a variety of experimental and computational biophysical approaches. Our findings indicate that SCR contains an amino acid segment at the C-terminal region that shows a remarkable affinity for cholesterol, although it lacks the CRAC sequence. Other 3-OH sterols, but not steroids lacking the 3-OH group, also bind this region of the protein. The newly identified cholesterol-binding region is located partly at the C-terminal portion of the TMD and partly in the first amino acid residues in the SCR C-terminal extracellular coil. This finding could be related to the previously described affinity of SCR for cholesterol-rich domains in membranes.Fil: Posada, Itziar M. D.. Universidad del País Vasco; EspañaFil: Fantini, Jacques. Universidad de Aix-Marsella; FranciaFil: Contreras, F. Xabier. Universidad del País Vasco; España. Ikerbasque; EspañaFil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas; ArgentinaFil: Alonso, Alicia. Universidad del País Vasco; EspañaFil: Goñi, Félix M.. Universidad del País Vasco; EspañaCell Press2014-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/98814Posada, Itziar M. D.; Fantini, Jacques; Contreras, F. Xabier; Barrantes, Francisco Jose; Alonso, Alicia; et al.; A cholesterol recognition motif in human phospholipid scramblase 1; Cell Press; Biophysical Journal; 107; 6; 9-2014; 1383-13920006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2014.07.039info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S000634951400784Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:26:21Zoai:ri.conicet.gov.ar:11336/98814instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:26:21.477CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A cholesterol recognition motif in human phospholipid scramblase 1
title A cholesterol recognition motif in human phospholipid scramblase 1
spellingShingle A cholesterol recognition motif in human phospholipid scramblase 1
Posada, Itziar M. D.
MEMBRANE PROTEIN
CHOLESTEROL
PROTEIN-LIPID INTERACTIONS
ENZYME
title_short A cholesterol recognition motif in human phospholipid scramblase 1
title_full A cholesterol recognition motif in human phospholipid scramblase 1
title_fullStr A cholesterol recognition motif in human phospholipid scramblase 1
title_full_unstemmed A cholesterol recognition motif in human phospholipid scramblase 1
title_sort A cholesterol recognition motif in human phospholipid scramblase 1
dc.creator.none.fl_str_mv Posada, Itziar M. D.
Fantini, Jacques
Contreras, F. Xabier
Barrantes, Francisco Jose
Alonso, Alicia
Goñi, Félix M.
author Posada, Itziar M. D.
author_facet Posada, Itziar M. D.
Fantini, Jacques
Contreras, F. Xabier
Barrantes, Francisco Jose
Alonso, Alicia
Goñi, Félix M.
author_role author
author2 Fantini, Jacques
Contreras, F. Xabier
Barrantes, Francisco Jose
Alonso, Alicia
Goñi, Félix M.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv MEMBRANE PROTEIN
CHOLESTEROL
PROTEIN-LIPID INTERACTIONS
ENZYME
topic MEMBRANE PROTEIN
CHOLESTEROL
PROTEIN-LIPID INTERACTIONS
ENZYME
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Human phospholipid scramblase 1 (SCR) catalyzes phospholipid transmembrane (flip-flop) motion. This protein is assumed to bind the membrane hydrophobic core through a transmembrane domain (TMD) as well as via covalently bound palmitoyl residues. Here, we explore the possible interaction of the SCR TMD with cholesterol by using a variety of experimental and computational biophysical approaches. Our findings indicate that SCR contains an amino acid segment at the C-terminal region that shows a remarkable affinity for cholesterol, although it lacks the CRAC sequence. Other 3-OH sterols, but not steroids lacking the 3-OH group, also bind this region of the protein. The newly identified cholesterol-binding region is located partly at the C-terminal portion of the TMD and partly in the first amino acid residues in the SCR C-terminal extracellular coil. This finding could be related to the previously described affinity of SCR for cholesterol-rich domains in membranes.
Fil: Posada, Itziar M. D.. Universidad del País Vasco; España
Fil: Fantini, Jacques. Universidad de Aix-Marsella; Francia
Fil: Contreras, F. Xabier. Universidad del País Vasco; España. Ikerbasque; España
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas; Argentina
Fil: Alonso, Alicia. Universidad del País Vasco; España
Fil: Goñi, Félix M.. Universidad del País Vasco; España
description Human phospholipid scramblase 1 (SCR) catalyzes phospholipid transmembrane (flip-flop) motion. This protein is assumed to bind the membrane hydrophobic core through a transmembrane domain (TMD) as well as via covalently bound palmitoyl residues. Here, we explore the possible interaction of the SCR TMD with cholesterol by using a variety of experimental and computational biophysical approaches. Our findings indicate that SCR contains an amino acid segment at the C-terminal region that shows a remarkable affinity for cholesterol, although it lacks the CRAC sequence. Other 3-OH sterols, but not steroids lacking the 3-OH group, also bind this region of the protein. The newly identified cholesterol-binding region is located partly at the C-terminal portion of the TMD and partly in the first amino acid residues in the SCR C-terminal extracellular coil. This finding could be related to the previously described affinity of SCR for cholesterol-rich domains in membranes.
publishDate 2014
dc.date.none.fl_str_mv 2014-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/98814
Posada, Itziar M. D.; Fantini, Jacques; Contreras, F. Xabier; Barrantes, Francisco Jose; Alonso, Alicia; et al.; A cholesterol recognition motif in human phospholipid scramblase 1; Cell Press; Biophysical Journal; 107; 6; 9-2014; 1383-1392
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/98814
identifier_str_mv Posada, Itziar M. D.; Fantini, Jacques; Contreras, F. Xabier; Barrantes, Francisco Jose; Alonso, Alicia; et al.; A cholesterol recognition motif in human phospholipid scramblase 1; Cell Press; Biophysical Journal; 107; 6; 9-2014; 1383-1392
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2014.07.039
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S000634951400784X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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