Formin-2 drives polymerisation of actin filaments enabling segregation of apicoplasts and cytokinesis in Plasmodium falciparum .

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Tytuł:: Formin-2 drives polymerisation of actin filaments enabling segregation of apicoplasts and cytokinesis in Plasmodium falciparum .
Autorzy:: Stortz JF; Wellcome Centre for Integrative Parasitology, Institute of Infection, Immunity & Inflammation, University of Glasgow, Glasgow, United Kingdom.
Del Rosario M; Wellcome Centre for Integrative Parasitology, Institute of Infection, Immunity & Inflammation, University of Glasgow, Glasgow, United Kingdom.
Singer M; Faculty of Veterinary Medicine, Experimental Parasitology, Ludwig Maximilian University, Munich, Germany.
Wilkes JM; Wellcome Centre for Integrative Parasitology, Institute of Infection, Immunity & Inflammation, University of Glasgow, Glasgow, United Kingdom.
Meissner M; Wellcome Centre for Integrative Parasitology, Institute of Infection, Immunity & Inflammation, University of Glasgow, Glasgow, United Kingdom.; Faculty of Veterinary Medicine, Experimental Parasitology, Ludwig Maximilian University, Munich, Germany.
Das S; Wellcome Centre for Integrative Parasitology, Institute of Infection, Immunity & Inflammation, University of Glasgow, Glasgow, United Kingdom.; Faculty of Veterinary Medicine, Experimental Parasitology, Ludwig Maximilian University, Munich, Germany.
Źródło:: ELife [Elife] 2019 Jul 19; Vol. 8. Date of Electronic Publication: 2019 Jul 19.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
MeSH Terms:: Actin Cytoskeleton/*metabolism
Cytokinesis/*genetics
Formins/*chemistry
Malaria, Falciparum/*genetics
Actin Cytoskeleton/chemistry ; Actins/genetics ; Actins/metabolism ; Apicoplasts/chemistry ; Apicoplasts/metabolism ; Endocytosis/genetics ; Erythrocytes/chemistry ; Erythrocytes/parasitology ; Formins/genetics ; Gene Expression Regulation/genetics ; Humans ; Malaria, Falciparum/metabolism ; Malaria, Falciparum/parasitology ; Plasmodium falciparum/chemistry ; Plasmodium falciparum/metabolism ; Protein Binding ; Toxoplasma/metabolism ; Toxoplasma/pathogenicity
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Grant Information:: ERC-2012-StG 309255-EndoTox International H2020 Excellent Science; Wellcome Senior Fellowship 103875/Z/14/Z International Wellcome; LMU Fellowship H2020-MSCA-COFUND-2016-754388 International Horizon 2020 Framework Programme; 085349 - Core funding for the WCMP International Wellcome; IFTH-GBE-2015-0475-M International National Secretariat for Higher Education, Sciences, Technology and Innovation of Ecuador (SENESCYT) PhD scholarship
Contributed Indexing:: Keywords: P. falciparum; Toxoplasma gondii; actin; apicoplast; cell biology; formin; infectious disease; malaria; microbiology; toxoplasmosis
Substance Nomenclature:: 0 (Actins)
0 (Formins)
Entry Date(s):: Date Created: 20190720 Date Completed: 20200219 Latest Revision: 20231013
Update Code:: 20240105
PubMed Central ID:: PMC6688858
DOI:: 10.7554/eLife.49030
PMID:: 31322501
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In addition to its role in erythrocyte invasion, Plasmodium falciparum actin is implicated in endocytosis, cytokinesis and inheritance of the chloroplast-like organelle called the apicoplast. Previously, the inability to visualise filamentous actin (F-actin) dynamics had restricted the characterisation of both F-actin and actin regulatory proteins, a limitation we recently overcame for Toxoplasma (Periz et al, 2017). Here, we have expressed and validated actin-binding chromobodies as F-actin-sensors in Plasmodium falciparum and characterised in-vivo actin dynamics. F-actin could be chemically modulated, and genetically disrupted upon conditionally deleting actin-1 . In a comparative approach, we demonstrate that Formin-2, a predicted nucleator of F-actin, is responsible for apicoplast inheritance in both Plasmodium and Toxoplasma , and additionally mediates efficient cytokinesis in Plasmodium . Finally, time-averaged local intensity measurements of F-actin in Toxoplasma conditional mutants revealed molecular determinants of spatiotemporally regulated F-actin flow. Together, our data indicate that Formin-2 is the primary F-actin nucleator during apicomplexan intracellular growth, mediating multiple essential functions.
Competing Interests: JS, MD, MS, JW, MM, SD No competing interests declared
(© 2019, Stortz et al.)

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