{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T20:25:54Z","timestamp":1768595154910,"version":"3.49.0"},"reference-count":57,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,10,16]],"date-time":"2014-10-16T00:00:00Z","timestamp":1413417600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI099493"],"award-info":[{"award-number":["R01 AI099493"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI073783"],"award-info":[{"award-number":["R01 AI073783"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI031940"],"award-info":[{"award-number":["R01 AI031940"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,11]]},"abstract":"Summary<\/jats:title>The catalytic A<\/jats:styled-content>1 subunit of cholera toxin (CTA1<\/jats:styled-content>) has a disordered structure at 37\u00b0C. An interaction with host factors must therefore place CTA1<\/jats:styled-content> in a folded conformation for the modification of its Gs<\/jats:styled-content>\u03b1 target which resides in a lipid raft environment. Host ADP<\/jats:styled-content>\u2010ribosylation factors (ARFs<\/jats:styled-content>) act as in vitro<\/jats:italic> allosteric activators of CTA1<\/jats:styled-content>, but the molecular events of this process are not fully characterized. Isotope\u2010edited F<\/jats:styled-content>ourier transform infrared spectroscopy monitored ARF6<\/jats:styled-content>\u2010induced structural changes to CTA1<\/jats:styled-content>, which were correlated to changes in CTA1<\/jats:styled-content> activity. We found ARF6<\/jats:styled-content> prevents the thermal disordering of structured CTA1<\/jats:styled-content> and stimulates the activity of stabilized CTA1<\/jats:styled-content> over a range of temperatures. Yet ARF6<\/jats:styled-content> alone did not promote the refolding of disordered CTA1<\/jats:styled-content> to an active state. Instead, lipid rafts shifted disordered CTA1<\/jats:styled-content> to a folded conformation with a basal level of activity that could be further stimulated by ARF6<\/jats:styled-content>. Thus, ARF<\/jats:styled-content> alone is unable to activate disordered CTA1<\/jats:styled-content> at physiological temperature: additional host factors such as lipid rafts place CTA1<\/jats:styled-content> in the folded conformation required for its ARF<\/jats:styled-content>\u2010mediated activation. Interaction with ARF<\/jats:styled-content> is required for in vivo<\/jats:italic> toxin activity, as enzymatically active CTA1<\/jats:styled-content> mutants that cannot be further stimulated by ARF6<\/jats:styled-content> fail to intoxicate cultured cells.<\/jats:p>","DOI":"10.1111\/mmi.12807","type":"journal-article","created":{"date-parts":[[2014,9,26]],"date-time":"2014-09-26T08:43:59Z","timestamp":1411721039000},"page":"898-912","source":"Crossref","is-referenced-by-count":21,"title":["ADP<\/scp>\u2010ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A<\/scp>1 polypeptide"],"prefix":"10.1111","volume":"94","author":[{"given":"Tuhina","family":"Banerjee","sequence":"first","affiliation":[{"name":"Burnett School of Biomedical Sciences College of Medicine University of Central Florida Orlando FL 32826 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