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Of the four known B subunits, the B\u201d\u2019 subunit (known as striatin) interacts with the multi-protein striatin-interacting phosphatase and kinase (STRIPAK) complex. Orthologs of STRIPAK components were identified in\n                    <jats:italic>Cryptococcus neoformans<\/jats:italic>\n                    , namely PP2AA\/Tpd3, PP2AC\/Pph22, PP2AB\/Far8, STRIP\/Far11, SLMAP\/Far9, and Mob3. Structural modeling, protein domain analysis, and detected protein-protein interactions suggest\n                    <jats:italic>C<\/jats:italic>\n                    .\n                    <jats:italic>neoformans<\/jats:italic>\n                    STRIPAK is assembled similarly to the human and fungal orthologs. Here, STRIPAK components Pph22, Far8, and Mob3 were functionally characterized. Whole-genome sequencing revealed that mutations in STRIPAK complex subunits lead to increased segmental and chromosomal aneuploidy, suggesting STRIPAK functions in maintaining genome stability. We demonstrate that\n                    <jats:italic>PPH22<\/jats:italic>\n                    is a haploinsufficient gene: heterozygous\n                    <jats:italic>PPH22\/pph22<\/jats:italic>\n                    \u0394 mutant diploid strains exhibit defects in hyphal growth and sporulation and have a significant fitness disadvantage when grown in competition against a wild-type diploid. Deletion mutants\n                    <jats:italic>pph22<\/jats:italic>\n                    \u0394,\n                    <jats:italic>far8<\/jats:italic>\n                    \u0394, and\n                    <jats:italic>mob3<\/jats:italic>\n                    \u0394 exhibit defects in mating and sexual differentiation, including impaired hyphae, basidia, and basidiospore production. Loss of either\n                    <jats:italic>PPH22<\/jats:italic>\n                    or\n                    <jats:italic>FAR8<\/jats:italic>\n                    in a haploid background leads to growth defects at 30\u00b0C, severely reduced growth at elevated temperature, abnormal cell morphology, and impaired virulence. Additionally,\n                    <jats:italic>pph22<\/jats:italic>\n                    \u0394 strains frequently accumulate suppressor mutations that result in overexpression of another putative PP2A catalytic subunit,\n                    <jats:italic>PPG1<\/jats:italic>\n                    . The\n                    <jats:italic>pph22<\/jats:italic>\n                    \u0394 and\n                    <jats:italic>far8<\/jats:italic>\n                    \u0394 mutants are also unable to grow in the presence of the calcineurin inhibitors cyclosporine A or FK506, and thus these mutations are synthetically lethal with loss of calcineurin activity. Conversely,\n                    <jats:italic>mob3<\/jats:italic>\n                    \u0394 mutants display increased thermotolerance, capsule production, and melanization, and are hypervirulent in a murine infection model. Taken together, these findings reveal that the\n                    <jats:italic>C<\/jats:italic>\n                    .\n                    <jats:italic>neoformans<\/jats:italic>\n                    STRIPAK complex plays an important role in genome stability, vegetative growth, sexual development, and virulence in this prominent human fungal pathogen.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1012735","type":"journal-article","created":{"date-parts":[[2024,11,19]],"date-time":"2024-11-19T13:37:04Z","timestamp":1732023424000},"page":"e1012735","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":34,"title":["The Cryptococcus neoformans STRIPAK complex controls genome stability, sexual development, and virulence"],"prefix":"10.1371","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0630-1045","authenticated-orcid":true,"given":"Patricia P.","family":"Peterson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jin-Tae","family":"Choi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ci","family":"Fu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leah E.","family":"Cowen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheng","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong-Sun","family":"Bahn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6369-5995","authenticated-orcid":true,"given":"Joseph","family":"Heitman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2024,11,19]]},"reference":[{"issue":"Pt 3","key":"ppat.1012735.ref001","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1042\/bj3530417","article-title":"Protein phosphatase 2A: a highly regulated family of serine\/threonine phosphatases implicated in cell growth and signalling","volume":"353","author":"V Janssens","year":"2001","journal-title":"Biochem 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