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The multiple functions of actin in apicomplexan parasites
Author(s) -
Das Sujaan,
Stortz Johannes Felix,
Meissner Markus,
Periz Javier
Publication year - 2021
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.13345
Subject(s) - biology , actin , actin binding protein , gene isoform , microbiology and biotechnology , cytoskeleton , cytokinesis , actin cytoskeleton , amino acid , function (biology) , genetics , cell , gene , cell division
Abstract The cytoskeletal protein actin is highly abundant and conserved in eukaryotic cells. It occurs in two different states‐ the globular (G‐actin) form, which can polymerise into the filamentous (F‐actin) form, fulfilling various critical functions including cytokinesis, cargo trafficking and cellular motility. In higher eukaryotes, there are several actin isoforms with nearly identical amino acid sequences. Despite the high level of amino acid identity, they display regulated expression patterns and unique non‐redundant roles. The number of actin isoforms together with conserved sequences may reflect the selective pressure exerted by scores of actin binding proteins (ABPs) in higher eukaryotes. In contrast, in many protozoans such as apicomplexan parasites which possess only a few ABPs, the regulatory control of actin and its multiple functions are still obscure. Here, we provide a summary of the regulation and biological functions of actin in higher eukaryotes and compare it with the current knowledge in apicomplexans. We discuss future experiments that will help us understand the multiple, critical roles of this fascinating system in apicomplexans.

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