Holding back the microfilamentuStructural insights into actin and the actin-monomer-binding proteins of apicomplexan parasites
Details
Publication Year 2012-05,Volume 64,Issue #5,Page 370-377
Journal Title
IUBMB LIFE
Publication Type
Journal Article
Abstract
Parasites from the phylum Apicomplexa are responsible for several major diseases of man, including malaria and toxoplasmosis. These highly motile protozoa use a conserved actomyosin-based mode of movement to power tissue traversal and host cell invasion. The mode termed as gliding motility relies on the dynamic turnover of actin, whose polymerisation state is controlled by a markedly limited number of identifiable regulators when compared with other eukaryotic cells. Recent studies of apicomplexan actin regulator structurein particular those of the core triad of monomer-binding proteins, actin-depolymerising factor/cofilin, cyclase-associated protein/Srv2, and profilinhave provided new insights into possible mechanisms of actin regulation in parasite cells, highlighting divergent structural features and functions to regulators from other cellular systems. Furthermore, the unusual nature of apicomplexan actin itself is increasingly coming into the spotlight. Here, we review recent advances in understanding of the structure and function of actin and its regulators in apicomplexan parasites. In particular we explore the paradox between there being an abundance of unpolymerised actin, its having a seemingly increased potential to form filaments relative to vertebrate actin, and the apparent lack of visible, stable filaments in parasite cells. 2012 IUBMB IUBMB Life, 2012
Publisher
WILEY-BLACKWELL
Keywords
malaria;Plasmodium;actin;microfilaments;cofilin;actin-depolymerising factor;cyclase-associated protein;profilin;coronin;formin;crystallography;protein structure
Research Division(s)
Infection And Immunity
Terms of Use/Rights Notice
Copyright © 2012 Wiley Periodicals, Inc


Creation Date: 2012-05-01 12:00:00
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