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

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 cel...

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Autores principales: Dal Col, Jessica, Lamberti, Marìa Julia, Nigro, Annunziata, Casolaro, Vincenzo, Fratta, Elisabetta, Steffan, Agostino, Montico, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9158361/
https://www.ncbi.nlm.nih.gov/pubmed/35650588
http://dx.doi.org/10.1186/s12964-022-00895-3
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author Dal Col, Jessica
Lamberti, Marìa Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
author_facet Dal Col, Jessica
Lamberti, Marìa Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
author_sort Dal Col, Jessica
collection PubMed
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. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12964-022-00895-3.
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spelling pubmed-91583612022-06-02 Phospholipid scramblase 1: a protein with multiple functions via multiple molecular interactors Dal Col, Jessica Lamberti, Marìa Julia Nigro, Annunziata Casolaro, Vincenzo Fratta, Elisabetta Steffan, Agostino Montico, Barbara Cell Commun Signal Review 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. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12964-022-00895-3. BioMed Central 2022-06-01 /pmc/articles/PMC9158361/ /pubmed/35650588 http://dx.doi.org/10.1186/s12964-022-00895-3 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Dal Col, Jessica
Lamberti, Marìa Julia
Nigro, Annunziata
Casolaro, Vincenzo
Fratta, Elisabetta
Steffan, Agostino
Montico, Barbara
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
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_short 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
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9158361/
https://www.ncbi.nlm.nih.gov/pubmed/35650588
http://dx.doi.org/10.1186/s12964-022-00895-3
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