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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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Detalles Bibliográficos
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
Descripción
Sumario: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.