Journal article
Biosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX)
HE Bullen, SC Charnaud, M Kalanon, DT Riglar, C Dekiwadia, N Kangwanrangsan, M Torii, T Tsuboi, J Baum, SA Ralph, AF Cowman, TF De Koning-Ward, BS Crabb, PR Gilsona
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012
Abstract
To survive within its host erythrocyte, Plasmodium falciparum must export hundreds of proteins across both its parasite plasma membrane and surrounding parasitophorous vacuole membrane, most of which are likely to use a protein complex known as PTEX (Plasmodium translocon of exported proteins). PTEX is a putative protein trafficking machinery responsible for the export of hundreds of proteins across the parasitophorous vacuole membrane and into the human host cell. Five proteins are known to comprise the PTEX complex, and in this study, three of the major stoichiometric components are investigated including HSP101 (a AAA+ ATPase), a protein of no known function termed PTEX150, and the appare..
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Grants
Awarded by Japan Society for the Promotion of Science
Funding Acknowledgements
This work was supported by Australian National Health and Medical Research Council Grants 516740, 533811, and 406601). Supported by a Pratt Foundation Scholarship through University of Melbourne. Supported by a National Health and Medical Research Council Career Development Fellowship award.