Phosphorylation-depended conformational changes in KAHRP of Palsmodium falciparum

ABSTRACT: This dataset contains phosphoproteomic data generated to characterize phosphorylation of the knob-associated histidine-rich protein (KAHRP) in Plasmodium falciparum-infected erythrocytes. The study investigates the role of KAHRP phosphorylation in regulating its stage-specific interaction with the erythrocyte membrane skeletal protein ankyrin and its contribution to knob biogenesis. Phosphoproteomic analysis identified phosphorylation sites in KAHRP, including sites within the FM2 domain implicated in ankyrin binding. The mass spectrometry data were integrated with biochemical, cell biological, super-resolution imaging, and computational analyses to investigate a phosphorylation-dependent mechanism controlling KAHRP–ankyrin association during intraerythrocytic parasite development. The deposited files comprise the mass spectrometry data and associated analysis files underlying the phosphoproteomic results reported in the accompanying manuscript.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Erythrocyte, Cell Culture

DISEASE(S): Plasmodium Falciparum Malaria

SUBMITTER: Frank Stein  

LAB HEAD: Michael Lanzer

PROVIDER: PXD083281 | Pride | 2026-10-12

REPOSITORIES: Pride