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rdf:type |
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lifeskim:mentions |
umls-concept:C0014780,
umls-concept:C0024530,
umls-concept:C0030498,
umls-concept:C0032148,
umls-concept:C0090388,
umls-concept:C0332281,
umls-concept:C0449432,
umls-concept:C0816871,
umls-concept:C1179435,
umls-concept:C1421563,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
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pubmed:issue |
2
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pubmed:dateCreated |
2011-1-10
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pubmed:abstractText |
The malaria parasite invades the terminally differentiated erythrocytes, where it grows and multiplies surrounded by a parasitophorous vacuole. Plasmodium blood stages translocate newly synthesized proteins outside the parasitophorous vacuole and direct them to various erythrocyte compartments, including the cytoskeleton and the plasma membrane. Here, we show that the remodeling of the host cell directed by the parasite also includes the recruitment of dematin, an actin-binding protein of the erythrocyte membrane skeleton and its repositioning to the parasite. Internalized dematin was found associated with Plasmodium 14-3-3, which belongs to a family of conserved multitask molecules. We also show that, in vitro, the dematin-14-3-3 interaction is strictly dependent on phosphorylation of dematin at Ser(124) and Ser(333), belonging to two 14-3-3 putative binding motifs. This study is the first report showing that a component of the erythrocyte spectrin-based membrane skeleton is recruited by the malaria parasite following erythrocyte infection.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1083-351X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
14
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1227-36
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21084299-14-3-3 Proteins,
pubmed-meshheading:21084299-Animals,
pubmed-meshheading:21084299-Blood Proteins,
pubmed-meshheading:21084299-Cell Fractionation,
pubmed-meshheading:21084299-Cyclic AMP,
pubmed-meshheading:21084299-Cytoskeletal Proteins,
pubmed-meshheading:21084299-Cytoskeleton,
pubmed-meshheading:21084299-Erythrocyte Membrane,
pubmed-meshheading:21084299-Malaria,
pubmed-meshheading:21084299-Mice,
pubmed-meshheading:21084299-Mice, Inbred Strains,
pubmed-meshheading:21084299-Organisms, Genetically Modified,
pubmed-meshheading:21084299-Phosphoproteins,
pubmed-meshheading:21084299-Phosphorylation,
pubmed-meshheading:21084299-Plasmodium berghei,
pubmed-meshheading:21084299-Plasmodium falciparum,
pubmed-meshheading:21084299-Protein Transport,
pubmed-meshheading:21084299-Recombinant Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Dematin, a component of the erythrocyte membrane skeleton, is internalized by the malaria parasite and associates with Plasmodium 14-3-3.
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pubmed:affiliation |
Dipartimento di Malattie Infettive, Istituto Superiore di Sanità, 00161 Rome, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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