Functional homo- and heterodimeric actin capping proteins from the malaria parasite.

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ID: 99798
2020
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Ranked #16 of 66 articles by views in Biochemical and biophysical research communications

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Abstract
Actin capping proteins belong to the core set of proteins minimally required for actin-based motility and are present in virtually all eukaryotic cells. They bind to the fast-growing barbed end of an actin filament, preventing addition and loss of monomers, thus restricting growth to the slow-growing pointed end. Actin capping proteins are usually heterodimers of two subunits. The Plasmodium orthologs are an exception, as their α subunits are able to form homodimers. We show here that, while the β subunit alone is unstable, the α subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the αα homo- and αβ heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical αβ heterodimers, although certain rearrangements at the interface must be required. Both homo- and heterodimers bind to actin filaments in a roughly equimolar ratio, indicating they may also bind other sites than barbed ends.
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bendes2020functionalbiochemical Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Bendes, Ábris Ádám;Chatterjee, Moon;Götte, Benjamin;Kursula, Petri;Kursula, Inari;
Journal Biochemical and biophysical research communications
Year 2020
DOI
S0006-291X(20)30400-9
URL
Keywords
malaria plasmodium actin heterodimer capping protein homodimer

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