Abstract
Members of the dynamin superfamily are big GTPases that have remained mostly unchanged throughout evolution and are primarily characterised as mechanochemical enzymes engaged in membrane scission processes. Due to its large GTPase domain, conserved dynamin M and GED domains, and dynamin-like protein subgroup membership, PfDYN2 is a member of the dynamin superfamily. PfDYN2 partially co-localized with markers for the parasite endoplasmic reticulum, Golgi apparatus, and apicoplast, indicating that it may be involved in vesicular trafficking and/or organelle fission events that have been associated with the final stages of the parasite's development in erythrocytes. The P. falciparum genome only contains two members of the dynamin superfamily, PfDYN2 and PfDYN1.
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