Phosphorylation of Plasmodium berghei derived phosphoproteins associated with the host erythrocyte membrane by the spectrin kinase.
Plasmodium berghei derived phosphoproteins are associated with the host erythrocyte membrane. Effectors of the phosphorylation reaction regulate the phosphorylation of the P. berghei derived proteins and spectrin in a similar manner. The spectrin kinase also phosphorylates the P. berghei phosphoproteins in a reconstituted reaction at the same site(s) as the endogenously phosphorylated proteins. These results indicate that a host protein kinase may regulate parasite phosphoproteins during malaria.
Wiser
M F
MF
MacArthur Center for Molecular Parasitology, Yale University School of Medicine, New Haven, CT 06510-8028.
D000818:Animals; D002413:Cations, Divalent; D004163:Diphosphoglyceric Acids / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism; D006790:Host-Parasite Interactions; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010962:Plasmodium berghei / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*
D002413:Cations, Divalent; D004163:Diphosphoglyceric Acids; D008565:Membrane Proteins; D010750:Phosphoproteins; D011494:Protein Kinases; C033464:spectrin kinase