Graphic model depicting the organization of KAHRP. (a) Dynamic association of KAHRP with ankyrin bridges. We propose that KAHRP initially binds to both the ankyrin bridge forming a ternary complex with ankyrin and spectrin and to the actin junctional complex during early ring stage development. We further propose that KAHRP then re-positions to the actin junctional complex as the parasite matures. Concomitantly, the knob spiral forms and the actin junctional complexes re-organize. Re-organization of the actin junctional complex would include uncapping and mining the actin proto-filaments to form long filaments connecting the knobs with the Maurer’s clefts (b) Model depicting KAHRP as an associated factor of the spiral scaffold. According to the model, KAHRP would “glue” additional components to the spiral scaffold. This would include PfEMP1, the spectrin filaments (via a quaternary complex consisting of the N-terminus of ß-spectrin and protein 4.1R), and the long actin filaments. A “glue-like” function would be consistent with the multi-modular binding properties of KAHRP. The KAHRP symbol indicates one or several KAHRP molecules.

Sanchez CP, Patra P, Chang SS, Karathanasis C, Hanebutte L, Kilian N, Cyrklaff M, Heilemann M, Schwarz US, Kudryashev M, Lanzer M. KAHRP dynamically relocalizes to remodeled actin junctions and associates with knob spirals in P. falciparum-infected erythrocytes. Mol Microbiol. 2021 PMID: 34514656.