<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Green JL</submitter><funding>Cancer Research UK</funding><funding>Francis Crick Institute</funding><funding>School of Life Sciences, University of Nottingham</funding><funding>Universitetet i Bergen</funding><funding>Medical Research Council</funding><funding>The Francis Crick Institute</funding><funding>Wellcome Trust</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>17857-17875</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5663884</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>292(43)</volume><pubmed_abstract>Myosin A (MyoA) is a Class XIV myosin implicated in gliding motility and host cell and tissue invasion by malaria parasites. MyoA is part of a membrane-associated protein complex called the glideosome, which is essential for parasite motility and includes the MyoA light chain myosin tail domain-interacting protein (MTIP) and several glideosome-associated proteins (GAPs). However, most studies of MyoA have focused on single stages of the parasite life cycle. We examined MyoA expression throughout the &lt;i>Plasmodium berghei&lt;/i> life cycle in both mammalian and insect hosts. In extracellular ookinetes, sporozoites, and merozoites, MyoA was located at the parasite periphery. In the sexual stages, zygote formation and initial ookinete differentiation precede MyoA synthesis and deposition, which </pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Compositional and expression analyses of the glideosome during the &amp;lt;i&amp;gt;Plasmodium&amp;lt;/i&amp;gt; life cycle reveal an additional myosin light chain required for maximum motility.</pubmed_title><pmcid>PMC5663884</pmcid><funding_grant_id>MR/K011782/1</funding_grant_id><funding_grant_id>10097</funding_grant_id><funding_grant_id>BB/N017609/1</funding_grant_id><funding_grant_id>FC001097</funding_grant_id><funding_grant_id>2015/13383-EVR</funding_grant_id><funding_grant_id>G0900278 MR/K011782/1</funding_grant_id><funding_grant_id>FC0001119</funding_grant_id><funding_grant_id>MR/N023048/1</funding_grant_id><funding_grant_id>FC001119</funding_grant_id><funding_grant_id>10119</funding_grant_id><funding_grant_id>G0900109</funding_grant_id><funding_grant_id>10015</funding_grant_id><funding_grant_id>G0900278</funding_grant_id><pubmed_authors>Stock J</pubmed_authors><pubmed_authors>Brady D</pubmed_authors><pubmed_authors>Ridzuan MAM</pubmed_authors><pubmed_authors>Vahokoski J</pubmed_authors><pubmed_authors>Wall RJ</pubmed_authors><pubmed_authors>Green JL</pubmed_authors><pubmed_authors>Knuepfer E</pubmed_authors><pubmed_authors>Stanway RR</pubmed_authors><pubmed_authors>Tewari R</pubmed_authors><pubmed_authors>Kursula I</pubmed_authors><pubmed_authors>Yusuf NA</pubmed_authors><pubmed_authors>Pires IP</pubmed_authors><pubmed_authors>Molloy JE</pubmed_authors><pubmed_authors>Moon RW</pubmed_authors><pubmed_authors>Howell SA</pubmed_authors><pubmed_authors>Martin SR</pubmed_authors><pubmed_authors>Holder AA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Compositional and expression analyses of the glideosome during the &amp;lt;i&amp;gt;Plasmodium&amp;lt;/i&amp;gt; life cycle reveal an additional myosin light chain required for maximum motility.</name><description>Myosin A (MyoA) is a Class XIV myosin implicated in gliding motility and host cell and tissue invasion by malaria parasites. MyoA is part of a membrane-associated protein complex called the glideosome, which is essential for parasite motility and includes the MyoA light chain myosin tail domain-interacting protein (MTIP) and several glideosome-associated proteins (GAPs). However, most studies of MyoA have focused on single stages of the parasite life cycle. We examined MyoA expression throughout the &lt;i>Plasmodium berghei&lt;/i> life cycle in both mammalian and insect hosts. In extracellular ookinetes, sporozoites, and merozoites, MyoA was located at the parasite periphery. In the sexual stages, zygote formation and initial ookinete differentiation precede MyoA synthesis and deposition, which </description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Oct</publication><modification>2026-04-30T00:49:54.081Z</modification><creation>2019-03-27T03:00:27Z</creation></dates><accession>S-EPMC5663884</accession><cross_references><pubmed>28893907</pubmed><doi>10.1074/jbc.M117.802769</doi></cross_references></HashMap>