Format

Send to

Choose Destination
J Biol Chem. 2015 Jan 16;290(3):1712-28. doi: 10.1074/jbc.M114.598094. Epub 2014 Nov 25.

The role of palmitoylation for protein recruitment to the inner membrane complex of the malaria parasite.

Author information

1
From the M. G. DeGroote Institute for Infectious Disease Research, Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
2
the Program in Molecular Structure and Function, Hospital for Sick Children, and Departments of Biochemistry and Molecular Genetics, University of Toronto, Toronto, Ontario M5G 0A4, Canada.
3
the Department of Biology/Chemistry, Biochemistry Section, University of Osnabrück, 49076 Osnabrück, Germany.
4
the Bernhard-Nocht-Institute for Tropical Medicine, 20359 Hamburg, Germany, and.
5
From the M. G. DeGroote Institute for Infectious Disease Research, Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario L8N 3Z5, Canada, the Bernhard-Nocht-Institute for Tropical Medicine, 20359 Hamburg, Germany, and.
6
From the M. G. DeGroote Institute for Infectious Disease Research, Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario L8N 3Z5, Canada, the Bernhard-Nocht-Institute for Tropical Medicine, 20359 Hamburg, Germany, and the Center for Structural Systems Biology, 22607 Hamburg, Germany tgilber@mcmaster.ca.

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.

KEYWORDS:

Inner Membrane Complex; Malaria; Membrane Trafficking; Palmitoyl Acyltransferase; Phylogenetics; Plasmodium; Protein Acylation

PMID:
25425642
PMCID:
PMC4340414
DOI:
10.1074/jbc.M114.598094
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center