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Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion

Author

Listed:
  • Mahmood M. Alam

    (MRC Toxicology Unit, University of Leicester, Hodgkin Building)

  • Lev Solyakov

    (MRC Toxicology Unit, University of Leicester, Hodgkin Building)

  • Andrew R. Bottrill

    (PNACL, Core Biotechnology Services, University of Leicester)

  • Christian Flueck

    (Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine)

  • Faiza A. Siddiqui

    (International Centre for Genetic Engineering and Biotechnology (ICGEB))

  • Shailja Singh

    (International Centre for Genetic Engineering and Biotechnology (ICGEB))

  • Sharad Mistry

    (PNACL, Core Biotechnology Services, University of Leicester)

  • Maria Viskaduraki

    (Bioinformatics and Biostatistics Support Hub (B/BASH), Core Biotechnology Services, Maurice Shock Building, University of Leicester)

  • Kate Lee

    (Bioinformatics and Biostatistics Support Hub (B/BASH), Core Biotechnology Services, Maurice Shock Building, University of Leicester)

  • Christine S. Hopp

    (Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine)

  • Chetan E. Chitnis

    (International Centre for Genetic Engineering and Biotechnology (ICGEB))

  • Christian Doerig

    (Monash University, Building 76)

  • Robert W. Moon

    (MRC National Institute for Medical Research)

  • Judith L. Green

    (MRC National Institute for Medical Research)

  • Anthony A. Holder

    (MRC National Institute for Medical Research)

  • David A. Baker

    (Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine)

  • Andrew B. Tobin

    (MRC Toxicology Unit, University of Leicester, Hodgkin Building)

Abstract

Our understanding of the key phosphorylation-dependent signalling pathways in the human malaria parasite, Plasmodium falciparum, remains rudimentary. Here we address this issue for the essential cGMP-dependent protein kinase, PfPKG. By employing chemical and genetic tools in combination with quantitative global phosphoproteomics, we identify the phosphorylation sites on 69 proteins that are direct or indirect cellular targets for PfPKG. These PfPKG targets include proteins involved in cell signalling, proteolysis, gene regulation, protein export and ion and protein transport, indicating that cGMP/PfPKG acts as a signalling hub that plays a central role in a number of core parasite processes. We also show that PfPKG activity is required for parasite invasion. This correlates with the finding that the calcium-dependent protein kinase, PfCDPK1, is phosphorylated by PfPKG, as are components of the actomyosin complex, providing mechanistic insight into the essential role of PfPKG in parasite egress and invasion.

Suggested Citation

  • Mahmood M. Alam & Lev Solyakov & Andrew R. Bottrill & Christian Flueck & Faiza A. Siddiqui & Shailja Singh & Sharad Mistry & Maria Viskaduraki & Kate Lee & Christine S. Hopp & Chetan E. Chitnis & Chri, 2015. "Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion," Nature Communications, Nature, vol. 6(1), pages 1-15, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8285
    DOI: 10.1038/ncomms8285
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