Targeting of the ring exported protein 1 to the Maurer's clefts is mediated by a two-phase process - PubMed (original) (raw)

Targeting of the ring exported protein 1 to the Maurer's clefts is mediated by a two-phase process

Matthew W A Dixon et al. Traffic. 2008 Aug.

Free article

Abstract

Early development of Plasmodium falciparum within the erythrocyte is characterized by the large-scale export of proteins to the host cell. In many cases, export is mediated by a short sequence called the Plasmodium export element (PEXEL) or vacuolar transport signal; however, a number of previously characterized exported proteins do not contain such an element. In this study, we investigated the mechanisms of export of the PEXEL-negative ring exported protein 1 (REX1). This protein localizes to the Maurer's clefts, parasite-induced structures in the host-cell cytosol. Transgenic parasites expressing green fluorescent protein-REX1 chimeras revealed that the single hydrophobic stretch plus an additional 10 amino acids mediate the export of REX1. Biochemical characterization of these chimeras indicated that REX1 was exported as a soluble protein. Inclusion of a sequence containing a predicted coiled-coil motif led to the correct localization of REX1 at the Maurer's clefts, suggesting that association with the clefts occurs at the final stage of protein export only. These results indicate that PEXEL-negative exported proteins can be exported in a soluble state and that sequences without any apparent resemblance to a PEXEL motif can mediate export across the parasitophorous vacuole membrane.

PubMed Disclaimer

Cited by

Malaria parasite proteins that remodel the host erythrocyte.
Maier AG, Cooke BM, Cowman AF, Tilley L. Maier AG, et al. Nat Rev Microbiol. 2009 May;7(5):341-54. doi: 10.1038/nrmicro2110. Nat Rev Microbiol. 2009. PMID: 19369950 Review.
PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes.
Morita M, Nagaoka H, Ntege EH, Kanoi BN, Ito D, Nakata T, Lee JW, Tokunaga K, Iimura T, Torii M, Tsuboi T, Takashima E. Morita M, et al. Sci Rep. 2018 Feb 27;8(1):3696. doi: 10.1038/s41598-018-22026-0. Sci Rep. 2018. PMID: 29487358 Free PMC article.
Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export.
Heiber A, Kruse F, Pick C, Grüring C, Flemming S, Oberli A, Schoeler H, Retzlaff S, Mesén-Ramírez P, Hiss JA, Kadekoppala M, Hecht L, Holder AA, Gilberger TW, Spielmann T. Heiber A, et al. PLoS Pathog. 2013;9(8):e1003546. doi: 10.1371/journal.ppat.1003546. Epub 2013 Aug 8. PLoS Pathog. 2013. PMID: 23950716 Free PMC article.
Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton.
Rug M, Cyrklaff M, Mikkonen A, Lemgruber L, Kuelzer S, Sanchez CP, Thompson J, Hanssen E, O'Neill M, Langer C, Lanzer M, Frischknecht F, Maier AG, Cowman AF. Rug M, et al. Blood. 2014 Nov 27;124(23):3459-68. doi: 10.1182/blood-2014-06-583054. Epub 2014 Aug 19. Blood. 2014. PMID: 25139348 Free PMC article.
Trafficking and Association of Plasmodium falciparum MC-2TM with the Maurer's Clefts.
Yadavalli R, Peterson JW, Drazba JA, Sam-Yellowe TY. Yadavalli R, et al. Pathogens. 2021 Apr 5;10(4):431. doi: 10.3390/pathogens10040431. Pathogens. 2021. PMID: 33916455 Free PMC article.

Targeting of the ring exported protein 1 to the Maurer's clefts is mediated by a two-phase process - PubMed (original) (raw)