The Role of Palmitoylation for Protein Recruitment to the Inner Membrane Complex of the Malaria Parasite Academic Article uri icon

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abstract

  • To survive and persist within its human host, the malaria parasite Plasmodium falciparum utilizes a battery of lineage-specific innovations to invade and multiply in human erythrocytes. With central roles in invasion and cytokinesis, the inner membrane complex, a Golgi-derived double membrane structure underlying the plasma membrane of the parasite, represents a unique and unifying structure characteristic to all organisms belonging to a large phylogenetic group called Alveolata. More than 30 structurally and phylogenetically distinct proteins are embedded in the IMC, where a portion of these proteins displays N-terminal acylation motifs. Although N-terminal myristoylation is catalyzed co-translationally within the cytoplasm of the parasite, palmitoylation takes place at membranes and is mediated by palmitoyl acyltransferases (PATs). Here, we identify a PAT (PfDHHC1) that is exclusively localized to the IMC. Systematic phylogenetic analysis of the alveolate PAT family reveals PfDHHC1 to be a member of a highly conserved, apicomplexan-specific clade of PATs. We show that during schizogony this enzyme has an identical distribution like two dual-acylated, IMC-localized proteins (PfISP1 and PfISP3). We used these proteins to probe into specific sequence requirements for IMC-specific membrane recruitment and their interaction with differentially localized PATs of the parasite.

authors

  • Wetzel, Johanna
  • Herrmann, Susann
  • Swapna, Lakshmipuram Seshadri
  • Prusty, Dhaneswar
  • Peter, Arun T John
  • Kono, Maya
  • Saini, Sidharth
  • Nellimarla, Srinivas
  • Wong, Tatianna Wai Ying
  • Wilcke, Louisa
  • Ramsay, Olivia
  • Cabrera, Ana
  • Biller, Laura
  • Heincke, Dorothee
  • Mossman, Karen
  • Spielmann, Tobias
  • Ungermann, Christian
  • Parkinson, John
  • Gilberger, Tim W

publication date

  • January 16, 2015

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