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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2020,6,2]]},"abstract":"<jats:p>\n                    Apicomplexan parasites use a specialized cilium structure called the apical complex to organize their secretory organelles and invasion machinery. The apical complex is integrally associated with both the parasite plasma membrane and an intermediate filament cytoskeleton called the inner-membrane complex (IMC). While the apical complex is essential to the parasitic lifestyle, little is known about the regulation of apical complex biogenesis. Here, we identify AC9 (apical cap protein 9), a largely intrinsically disordered component of the\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    IMC, as essential for apical complex development, and therefore for host cell invasion and egress. Parasites lacking AC9 fail to successfully assemble the tubulin-rich core of their apical complex, called the conoid. We use proximity biotinylation to identify the AC9 interaction network, which includes the kinase extracellular signal-regulated kinase 7 (ERK7). Like AC9, ERK7 is required for apical complex biogenesis. We demonstrate that AC9 directly binds ERK7 through a conserved C-terminal motif and that this interaction is essential for ERK7 localization and function at the apical cap. The crystal structure of the ERK7\u2013AC9 complex reveals that AC9 is not only a scaffold but also inhibits ERK7 through an unusual set of contacts that displaces nucleotide from the kinase active site. ERK7 is an ancient and autoactivating member of the mitogen-activated kinase (MAPK) family and its regulation is poorly understood in all organisms. We propose that AC9 dually regulates ERK7 by scaffolding and concentrating it at its site of action while maintaining it in an \u201coff\u201d state until the specific binding of a true substrate.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1921245117","type":"journal-article","created":{"date-parts":[[2020,5,14]],"date-time":"2020-05-14T20:00:19Z","timestamp":1589486419000},"page":"12164-12173","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":60,"title":["Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required for\n                    <i>Toxoplasma<\/i>\n                    apical complex biogenesis"],"prefix":"10.1073","volume":"117","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4653-8602","authenticated-orcid":false,"given":"Peter S.","family":"Back","sequence":"first","affiliation":[{"name":"Molecular Biology Institute, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William J.","family":"O\u2019Shaughnessy","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4559-5530","authenticated-orcid":false,"given":"Andy S.","family":"Moon","sequence":"additional","affiliation":[{"name":"Department of Molecular Microbiology and Immunology, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pravin S.","family":"Dewangan","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyu","family":"Hu","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jihui","family":"Sha","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Wohlschlegel","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8481-0638","authenticated-orcid":false,"given":"Peter J.","family":"Bradley","sequence":"additional","affiliation":[{"name":"Molecular Biology Institute, University of California, Los Angeles, CA 90095;"},{"name":"Department of Molecular Microbiology and Immunology, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9401-9594","authenticated-orcid":false,"given":"Michael L.","family":"Reese","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390;"},{"name":"Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2020,5,14]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1038\/nrm.2017.60","article-title":"Genes and molecular pathways underpinning ciliopathies","volume":"18","author":"Reiter J. F.","year":"2017","unstructured":"J. F. Reiter, M. R. Leroux, Genes and molecular pathways underpinning ciliopathies. Nat. Rev. Mol. Cell Biol. 18, 533\u2013547 (2017).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"a021998","DOI":"10.1101\/cshperspect.a021998","article-title":"Intraflagellar transport and ciliary dynamics","volume":"9","author":"Ishikawa H.","year":"2017","unstructured":"H. Ishikawa, W. F. Marshall, Intraflagellar transport and ciliary dynamics. Cold Spring Harb. Perspect. Biol. 9, a021998 (2017).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"3789","DOI":"10.1242\/jcs.203505","article-title":"Maintaining centrosomes and cilia","volume":"130","author":"Werner S.","year":"2017","unstructured":"S. Werner, A. Pimenta-Marques, M. Bettencourt-Dias, Maintaining centrosomes and cilia. J. 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Wall ., SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector. Sci. Rep. 6, 28604 (2016).","journal-title":"Sci. Rep."},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s13630-016-0025-5","article-title":"Basal body structure and composition in the apicomplexans Toxoplasma and Plasmodium","volume":"5","author":"Francia M. E.","year":"2016","unstructured":"M. E. Francia, J.-F. Dubremetz, N. S. Morrissette, Basal body structure and composition in the apicomplexans Toxoplasma and Plasmodium. Cilia 5, 3 (2016).","journal-title":"Cilia"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"e1001444","DOI":"10.1371\/journal.pbio.1001444","article-title":"Cell division in apicomplexan parasites is organized by a homolog of the striated rootlet fiber of algal flagella","volume":"10","author":"Francia M. E.","year":"2012","unstructured":"M. E. 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