Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation

Autor: Anwar Ahmed, Tim W. Gilberger, Divya Catherine Thomas, Pushkar Sharma
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Erythrocytes
Gliding motility
Protozoan Proteins
lcsh:Medicine
Protozoology
Biochemistry
Molecular Cell Biology
Malaria
Falciparum
Phosphorylation
lcsh:Science
Cells
Cultured
Calcium signaling
0303 health sciences
Multidisciplinary
Kinase
030302 biochemistry & molecular biology
3. Good health
Cell biology
Host-Pathogen Interaction
Research Article
Signal Transduction
Recombinant Fusion Proteins
Plasmodium falciparum
chemistry.chemical_element
Calcium
Biology
Protein Chemistry
Microbiology
03 medical and health sciences
parasitic diseases
Humans
Calcium Signaling
Protein Interactions
Microbial Pathogens
Protein kinase B
030304 developmental biology
Phospholipase C
lcsh:R
Membrane Proteins
Proteins
biology.organism_classification
chemistry
Type C Phospholipases
Parastic Protozoans
lcsh:Q
Protein Kinases
Zdroj: PLoS ONE, Vol 7, Iss 4, p e35855 (2012)
PLoS ONE
ISSN: 1932-6203
Popis: The actomyosin motor complex of the glideosome provides the force needed by apicomplexan parasites such as Toxoplasma gondii (Tg) and Plasmodium falciparum (Pf) to invade their host cells and for gliding motility of their motile forms. Glideosome Associated Protein 45 (PfGAP45) is an essential component of the glideosome complex as it facilitates anchoring and effective functioning of the motor. Dissection of events that regulate PfGAP45 may provide insights into how the motor and the glideosome operate. We found that PfGAP45 is phosphorylated in response to Phospholipase C (PLC) and calcium signaling. It is phosphorylated by P. falciparum kinases Protein Kinase B (PfPKB) and Calcium Dependent Protein Kinase 1 (PfCDPK1), which are calcium dependent enzymes, at S89, S103 and S149. The Phospholipase C pathway influenced the phosphorylation of S103 and S149. The phosphorylation of PfGAP45 at these sites is differentially regulated during parasite development. The localization of PfGAP45 and its association may be independent of the phosphorylation of these sites. PfGAP45 regulation in response to calcium fits in well with the previously described role of calcium in host cell invasion by malaria parasite.
Databáze: OpenAIRE
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