期刊
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
卷 184, 期 2, 页码 99-108出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2012.05.002
关键词
Toxoplasma; Inner membrane complex; ISP; Palmitoylation; Myristoylation; Endodyogeny
资金
- Whitcome Undergraduate Research Fellowship
- UCLA URSP (Milton Got-tlieb Foundation)
- NIH [R01 (AI064616), R01 (AI081924)]
- Microbial Pathogenesis Training Grant [T32-AI07323]
Apicomplexan parasites utilize a peripheral membrane system called the inner membrane complex (IMC) to facilitate host cell invasion and parasite replication. We recently identified a novel family of Toxoplasma IMC Sub-compartment Proteins (ISP1/2/3) that localize to sub-domains of the IMC using a targeting mechanism that is dependent on coordinated myristoylation and palmitoylation of a series of residues in the N-terminus of the protein. While the precise functions of the ISPs are unknown, deletion of ISP2 results in replication defects, suggesting that this family of proteins plays a role in daughter cell formation. Here we have characterized a fourth ISP family member (ISP4) and discovered that this protein localizes to the central IMC sub-compartment, similar to ISP2. Like ISP1/3, ISP4 is dispensable for the tachyzoite lytic cycle as the disruption of ISP4 does not produce any gross replication or growth defects. Surprisingly, targeting of ISP4 to the IMC membranes is dependent on residues predicted for palmitoylation but not myristoylation, setting its trafficking apart from the other ISP proteins and demonstrating distinct mechanisms of protein localization to the IMC membranes, even within a family of highly related proteins. (C) 2012 Elsevier B.V. All rights reserved.
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