{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,6]],"date-time":"2026-02-06T22:17:20Z","timestamp":1770416240140,"version":"3.49.0"},"reference-count":66,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2016,12,23]],"date-time":"2016-12-23T00:00:00Z","timestamp":1482451200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>When <jats:italic>Toxoplasma gondii<\/jats:italic> egresses from the host cell, glyceraldehyde\u20103\u2010phosphate dehydrogenase 1 (GAPDH1), which is primary a glycolysis enzyme but actually a quintessential multifunctional protein, translocates to the unique cortical membrane skeleton. Here, we report the 2.25 \u00c5 resolution crystal structure of the GAPDH1 holoenzyme in a quaternary complex providing the basis for the molecular dissection of GAPDH1 structure\u2013function relationships Knockdown of GAPDH1 expression and catalytic site disruption validate the essentiality of GAPDH1 in intracellular replication but we confirmed that glycolysis is not strictly essential. We identify, for the first time, S\u2010loop phosphorylation as a novel, critical regulator of enzymatic activity that is consistent with the notion that the S\u2010loop is critical for cofactor binding, allosteric activation and oligomerization. We show that neither enzymatic activity nor phosphorylation state correlate with the ability to translocate to the cortex. However, we demonstrate that association of GAPDH1 with the cortex is mediated by the N\u2010terminus, likely palmitoylation. Overall, glycolysis and cortical translocation are functionally decoupled by post\u2010translational modifications.<\/jats:p>","DOI":"10.1111\/mmi.13577","type":"journal-article","created":{"date-parts":[[2016,11,17]],"date-time":"2016-11-17T23:16:48Z","timestamp":1479424608000},"page":"618-634","source":"Crossref","is-referenced-by-count":18,"title":["Membrane skeletal association and post\u2010translational allosteric regulation of <i>Toxoplasma gondii<\/i> GAPDH1"],"prefix":"10.1111","volume":"103","author":[{"given":"Rashmi","family":"Dubey","sequence":"first","affiliation":[{"name":"Department of Biology Boston College  MA 02467 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bart L.","family":"Staker","sequence":"additional","affiliation":[{"name":"Seattle Structural Genomics Center for Infectious Disease Seattle WA 98109 USA"},{"name":"The Center for Infectious Disease Research, Seattle (Formerly Seattle BioMed)  WA 98109 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ian T.","family":"Foe","sequence":"additional","affiliation":[{"name":"Department of Pathology Stanford University School of Medicine Stanford CA 55324 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew","family":"Bogyo","sequence":"additional","affiliation":[{"name":"Department of Pathology Stanford University School of Medicine Stanford CA 55324 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter J.","family":"Myler","sequence":"additional","affiliation":[{"name":"Seattle Structural Genomics Center for Infectious Disease Seattle WA 98109 USA"},{"name":"The Center for Infectious Disease Research, Seattle (Formerly Seattle BioMed)  WA 98109 USA"},{"name":"Department of Global Health and Department of Biomedical Informatics &amp; Medical Education University of Washington Seattle WA 98195 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hu\u00e2n 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