Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors

Autores
Dal Col, Jessica; Lamberti, María Julia; Nigro, Annunziata; Casolaro, Vincenzo; Fratta, Elisabetta; Steffan, Agostino; Montico, Barbara
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Phospholipid scramblase 1 (PLSCR1) is the most studied protein of the scramblase family. Originally, it was identified as a membrane protein involved in maintaining plasma membrane asymmetry. However, studies conducted over the past few years have shown the involvement of PLSCR1 in several other cellular pathways. Indeed, PLSCR1 is not only embedded in the plasma membrane but is also expressed in several intracellular compartments where it interacts with a diverse repertoire of effectors, mediators, and regulators contributing to distinct cellular processes. Although most PLSCR1 interactors are thought to be cell-type specific, PLSCR1 often exerts its regulatory functions through shared mechanisms, including the trafficking of different molecules within intracellular vesicles such as endosomes, liposomes, and phagosomes. Intriguingly, besides endogenous proteins, PLSCR1 was also reported to interact with exogenous viral proteins, thereby regulating viral uptake and spread. This review aims to summarize the current knowledge about the multiple roles of PLSCR1 in distinct cellular pathways. [MediaObject not available: see fulltext.].
Fil: Dal Col, Jessica. Universita di Salerno; Italia
Fil: Lamberti, María Julia. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Nigro, Annunziata. Universita di Salerno; Italia
Fil: Casolaro, Vincenzo. Universita di Salerno; Italia
Fil: Fratta, Elisabetta. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
Fil: Steffan, Agostino. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
Fil: Montico, Barbara. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
Materia
PLSCR1
Protein?protein interaction
Cell death
Infammation
Virus
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:11336/202071
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactorsDal Col, JessicaLamberti, María JuliaNigro, AnnunziataCasolaro, VincenzoFratta, ElisabettaSteffan, AgostinoMontico, BarbaraPLSCR1Protein?protein interactionCell deathInfammationVirushttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Phospholipid scramblase 1 (PLSCR1) is the most studied protein of the scramblase family. Originally, it was identified as a membrane protein involved in maintaining plasma membrane asymmetry. However, studies conducted over the past few years have shown the involvement of PLSCR1 in several other cellular pathways. Indeed, PLSCR1 is not only embedded in the plasma membrane but is also expressed in several intracellular compartments where it interacts with a diverse repertoire of effectors, mediators, and regulators contributing to distinct cellular processes. Although most PLSCR1 interactors are thought to be cell-type specific, PLSCR1 often exerts its regulatory functions through shared mechanisms, including the trafficking of different molecules within intracellular vesicles such as endosomes, liposomes, and phagosomes. Intriguingly, besides endogenous proteins, PLSCR1 was also reported to interact with exogenous viral proteins, thereby regulating viral uptake and spread. This review aims to summarize the current knowledge about the multiple roles of PLSCR1 in distinct cellular pathways. [MediaObject not available: see fulltext.].Fil: Dal Col, Jessica. Universita di Salerno; ItaliaFil: Lamberti, María Julia. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaFil: Nigro, Annunziata. Universita di Salerno; ItaliaFil: Casolaro, Vincenzo. Universita di Salerno; ItaliaFil: Fratta, Elisabetta. Centro Di Riferimento Oncologico Di Aviano (cro); ItaliaFil: Steffan, Agostino. Centro Di Riferimento Oncologico Di Aviano (cro); ItaliaFil: Montico, Barbara. Centro Di Riferimento Oncologico Di Aviano (cro); ItaliaBioMed Central2022-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/202071Dal Col, Jessica; Lamberti, María Julia; Nigro, Annunziata; Casolaro, Vincenzo; Fratta, Elisabetta; et al.; Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors; BioMed Central; Cell Communication and Signaling; 20; 1; 6-2022; 78-931478-811XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biosignaling.biomedcentral.com/articles/10.1186/s12964-022-00895-3info:eu-repo/semantics/altIdentifier/doi/10.1186/s12964-022-00895-3info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:46:02Zoai:ri.conicet.gov.ar:11336/202071instacron: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:34982025-10-22 11:46:03.281CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
title Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
spellingShingle Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
Dal Col, Jessica
PLSCR1
Protein?protein interaction
Cell death
Infammation
Virus
title_short Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
title_full Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
title_fullStr Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
title_full_unstemmed Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
title_sort Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors
dc.creator.none.fl_str_mv Dal Col, Jessica
Lamberti, María Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
author Dal Col, Jessica
author_facet Dal Col, Jessica
Lamberti, María Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
author_role author
author2 Lamberti, María Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv PLSCR1
Protein?protein interaction
Cell death
Infammation
Virus
topic PLSCR1
Protein?protein interaction
Cell death
Infammation
Virus
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Phospholipid scramblase 1 (PLSCR1) is the most studied protein of the scramblase family. Originally, it was identified as a membrane protein involved in maintaining plasma membrane asymmetry. However, studies conducted over the past few years have shown the involvement of PLSCR1 in several other cellular pathways. Indeed, PLSCR1 is not only embedded in the plasma membrane but is also expressed in several intracellular compartments where it interacts with a diverse repertoire of effectors, mediators, and regulators contributing to distinct cellular processes. Although most PLSCR1 interactors are thought to be cell-type specific, PLSCR1 often exerts its regulatory functions through shared mechanisms, including the trafficking of different molecules within intracellular vesicles such as endosomes, liposomes, and phagosomes. Intriguingly, besides endogenous proteins, PLSCR1 was also reported to interact with exogenous viral proteins, thereby regulating viral uptake and spread. This review aims to summarize the current knowledge about the multiple roles of PLSCR1 in distinct cellular pathways. [MediaObject not available: see fulltext.].
Fil: Dal Col, Jessica. Universita di Salerno; Italia
Fil: Lamberti, María Julia. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Nigro, Annunziata. Universita di Salerno; Italia
Fil: Casolaro, Vincenzo. Universita di Salerno; Italia
Fil: Fratta, Elisabetta. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
Fil: Steffan, Agostino. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
Fil: Montico, Barbara. Centro Di Riferimento Oncologico Di Aviano (cro); Italia
description Phospholipid scramblase 1 (PLSCR1) is the most studied protein of the scramblase family. Originally, it was identified as a membrane protein involved in maintaining plasma membrane asymmetry. However, studies conducted over the past few years have shown the involvement of PLSCR1 in several other cellular pathways. Indeed, PLSCR1 is not only embedded in the plasma membrane but is also expressed in several intracellular compartments where it interacts with a diverse repertoire of effectors, mediators, and regulators contributing to distinct cellular processes. Although most PLSCR1 interactors are thought to be cell-type specific, PLSCR1 often exerts its regulatory functions through shared mechanisms, including the trafficking of different molecules within intracellular vesicles such as endosomes, liposomes, and phagosomes. Intriguingly, besides endogenous proteins, PLSCR1 was also reported to interact with exogenous viral proteins, thereby regulating viral uptake and spread. This review aims to summarize the current knowledge about the multiple roles of PLSCR1 in distinct cellular pathways. [MediaObject not available: see fulltext.].
publishDate 2022
dc.date.none.fl_str_mv 2022-06
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/11336/202071
Dal Col, Jessica; Lamberti, María Julia; Nigro, Annunziata; Casolaro, Vincenzo; Fratta, Elisabetta; et al.; Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors; BioMed Central; Cell Communication and Signaling; 20; 1; 6-2022; 78-93
1478-811X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/202071
identifier_str_mv Dal Col, Jessica; Lamberti, María Julia; Nigro, Annunziata; Casolaro, Vincenzo; Fratta, Elisabetta; et al.; Phospholipid scramblase 1: A protein with multiple functions via multiple molecular interactors; BioMed Central; Cell Communication and Signaling; 20; 1; 6-2022; 78-93
1478-811X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://biosignaling.biomedcentral.com/articles/10.1186/s12964-022-00895-3
info:eu-repo/semantics/altIdentifier/doi/10.1186/s12964-022-00895-3
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 BioMed Central
publisher.none.fl_str_mv BioMed Central
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 12.982451

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