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Calcineurin is a serine\/threonine phosphatase that is widely conserved across eukaryotes. When calcineurin function is inhibited in\n                    <jats:italic>Mucor<\/jats:italic>\n                    , growth shifts to a less virulent yeast growth form, which makes calcineurin an attractive target for development of new antifungal drugs. Previously, we identified two distinct mechanisms through which\n                    <jats:italic>Mucor<\/jats:italic>\n                    can become resistant to calcineurin inhibitors involving Mendelian mutations in the gene for FKBP12, including mechanisms corresponding to calcineurin A or B subunits and epimutations silencing the FKBP12 gene. Here, we identified a third novel mechanism where loss-of-function mutations in the amino acid permease corresponding to the\n                    <jats:italic>bycA<\/jats:italic>\n                    gene contribute to resistance against calcineurin inhibitors. When calcineurin activity is absent, BycA can activate protein kinase A (PKA) to promote yeast growth via a cAMP-independent pathway. Our data also show that calcineurin activity contributes to host-pathogen interactions primarily in the pathogenesis of\n                    <jats:italic>Mucor.<\/jats:italic>\n                  <\/jats:p>","DOI":"10.1128\/mbio.02949-19","type":"journal-article","created":{"date-parts":[[2020,1,27]],"date-time":"2020-01-27T05:21:52Z","timestamp":1580102512000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":44,"title":["A Novel Resistance Pathway for Calcineurin Inhibitors in the Human-Pathogenic Mucorales Mucor circinelloides"],"prefix":"10.1128","volume":"11","author":[{"given":"Sandeep","family":"Vellanki","sequence":"first","affiliation":[{"name":"South Texas Center for Emerging Infectious Diseases (STCEID), Department of Biology, The University of Texas at San Antonio, San Antonio, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. 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