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Emerging roles of the Protein Phosphatase 1 (PP1) in the context of viral infections.
Corda, Pedro O; Bollen, Mathieu; Ribeiro, Daniela; Fardilha, Margarida.
Affiliation
  • Corda PO; Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, Aveiro, Portugal.
  • Bollen M; Department of Cellular and Molecular Medicine, Laboratory of Biosignaling & Therapeutics, Katholieke Universiteit Leuven, Louvain, Belgium.
  • Ribeiro D; Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, Aveiro, Portugal. daniela.ribeiro@ua.pt.
  • Fardilha M; Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, Aveiro, Portugal. mfardilha@ua.pt.
Cell Commun Signal ; 22(1): 65, 2024 01 24.
Article in En | MEDLINE | ID: mdl-38267954
ABSTRACT
Protein Phosphatase 1 (PP1) is a major serine/threonine phosphatase in eukaryotes, participating in several cellular processes and metabolic pathways. Due to their low substrate specificity, PP1's catalytic subunits do not exist as free entities but instead bind to Regulatory Interactors of Protein Phosphatase One (RIPPO), which regulate PP1's substrate specificity and subcellular localization. Most RIPPOs bind to PP1 through combinations of short linear motifs (4-12 residues), forming highly specific PP1 holoenzymes. These PP1-binding motifs may, hence, represent attractive targets for the development of specific drugs that interfere with a subset of PP1 holoenzymes. Several viruses exploit the host cell protein (de)phosphorylation machinery to ensure efficient virus particle formation and propagation. While the role of many host cell kinases in viral life cycles has been extensively studied, the targeting of phosphatases by viral proteins has been studied in less detail. Here, we compile and review what is known concerning the role of PP1 in the context of viral infections and discuss how it may constitute a putative host-based target for the development of novel antiviral strategies.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Diseases / Protein Processing, Post-Translational Limits: Humans Language: En Journal: Cell Commun Signal Year: 2024 Document type: Article Affiliation country: Portugal

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Diseases / Protein Processing, Post-Translational Limits: Humans Language: En Journal: Cell Commun Signal Year: 2024 Document type: Article Affiliation country: Portugal