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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/202071
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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 Técnicas2025-09-29T10:15:53Zoai: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:34982025-09-29 10:15:53.812CONICET 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 |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |