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|Title:||Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion|
|Authors:||Alam, Mahmood M.|
Bottrill, Andrew R.
Siddiqui, F. A.
Hopp, C. S.
Chitnis, C. E.
Moon, R. W.
Green, J. L.
Holder, A. A.
Baker, D. A.
Tobin, Andrew B.
|Publisher:||Nature Publishing Group|
|Citation:||Nature Communications 6:7285|
|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.|
|Version:||Published article (publisher version)|
|Rights:||This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/|
|Appears in Collections:||Published Articles, Dept. of Cell Physiology and Pharmacology|
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