title: The measles virus phosphoprotein interacts with the linker domain of STAT1.
abstract: The measles virus (MV) phosphoprotein (P) and V proteins block the interferon (IFN) response by impeding phosphorylation of the signal transducer and activator of transcription 1 (STAT1) by the Janus kinase 1 (JAK1). We characterized how STAT1 mutants interact with P and JAK1 phosphorylation. Certain mutants of the linker, the Src-homology 2 domain (SH2), or the transactivation domain had reduced or abolished phosphorylation through JAK1 after IFN treatment. Other mutants, mainly localized in the linker, failed to interact with P as documented by the lack of interference with nuclear translocation. Thus the functional footprint of P on STAT1 localizes mainly to the linker domain; there is also some overlap with the STAT1 phosphorylation functional footprint on the SH2 domain. Based on these observations, we discuss how the MV-P might operate to inhibit the JAK/STAT pathway.
authors.affiliation: Department of Molecular Medicine, and Virology and Gene Therapy Graduate Track, Mayo Clinic College of Medicine, Rochester, MN 55905, USA. devaux.patricia@mayo.edu
authors.forename: Patricia
authors.initials: P
authors.lastname: Devaux
authors.forename: Lauren
authors.initials: L
authors.lastname: Priniski
authors.forename: Roberto
authors.initials: R
authors.lastname: Cattaneo
mesh_terms: D002460:Cell Line; D004252:DNA Mutational Analysis; D054884:Host-Pathogen Interactions; D006801:Humans; D008459:Measles virus / Q000502:physiology*; D010750:Phosphoproteins / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D050794:STAT1 Transcription Factor / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: C055859:P protein, Sendai virus; D010750:Phosphoproteins; D050794:STAT1 Transcription Factor; C494079:STAT1 protein, human; D014764:Viral Proteins
keywords: Innate immunity; Interferon signaling; Measles virus; Phosphoprotein; STAT1