Yersinia effector protein (YopO)-mediated phosphorylation of host gelsolin causes calcium-independent activation leading to disruption of actin dynamics

• Main Authors: Singaravelu P., Lee W.L., Wee S., Ghoshdastider U., Ding K., Gunaratne J., Grimes J.M., Swaminathan K., Robinson R.C.
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: American Society for Biochemistry and Molecular Biology Inc. 2020
• Subjects: Amino acids; Antigen-antibody reactions; Calcium; Chemical activation; Dynamics; Mass spectrometry; Phosphorylation; Actin dynamics; Actin polymerization; Calcium dependent; Gelsolin homology domain; Open conformation; Phagocytic cells; Phosphorylation sites; Yersinia pestis; Proteins; bacterial protein; gelsolin; unclassified drug; Yersinia effector protein; actin; calcium; protein serine threonine kinase; pyrene; pyrene derivative; serine; threonine; YopO protein, Yersinia enterocolitica; actin filament; Article; cell disruption; controlled study; mass spectrometry; nonhuman; phagocyte; phagocytosis; priority journal; protein binding; protein domain; protein function; protein modification; protein phosphorylation; protein polymerization; protein synthesis regulation; sequence homology; binding site; chemistry; human; macrophage; metabolism; microbiology; molecular dynamics; mutation; phosphorylation; Yersinia; Actin Cytoskeleton; Actins; Bacterial Proteins; Binding Sites; Gelsolin; Humans; Macrophages; Mass Spectrometry; Molecular Dynamics Simulation; Mutation; Phagocytosis; Protein Domains; Protein-Serine-Threonine Kinases; Pyrenes; Serine; Threonine
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/175223
• Institution: National University of Singapore

10.1074/jbc.M116.757971