Jin, Jae-Hyung Lee, Kyung-Tae Hong, Joohyeon Lee, Dongpil Jang, Eun-Ha Kim, Jin-Young Lee, Yeonseon Lee, Seung-Heon So, Yee-Seul Jung, Kwang-Woo Lee, Dong-Gi Jeong, Eunji Lee, Minjae Jang, Yu-Byeong Choi, Yeseul Lee, Myung Ha Kim, Ji-Seok Yu, Seong-Ryong Choi, Jin-Tae La, Jae-Won Choi, Haneul Kim, Sun-Woo Seo, Kyung Jin Lee, Yelin Thak, Eun Jung Choi, Jaeyoung Averette, Anna F. Lee, Yong-Hwan Heitman, Joseph Kang, Hyun Ah Cheong, Eunji Bahn, Yong-Sun 2024-01-19T17:02:18Z 2024-01-19T17:02:18Z 2021-09-02 2020-08 2041-1723 https://pubs.kist.re.kr/handle/201004/118331 Phosphatases, together with kinases and transcription factors, are key components in cellular signalling networks. Here, we present a systematic functional analysis of the phosphatases in Cryptococcus neoformans, a fungal pathogen that causes life-threatening fungal meningoencephalitis. We analyse 230 signature-tagged mutant strains for 114 putative phosphatases under 30 distinct in vitro growth conditions, revealing at least one function for 60 of these proteins. Large-scale virulence and infectivity assays using insect and mouse models indicate roles in pathogenicity for 31 phosphatases involved in various processes such as thermotolerance, melanin and capsule production, stress responses, O-mannosylation, or retromer function. Notably, phosphatases Xpp1, Ssu72, Siw14, and Sit4 promote blood-brain barrier adhesion and crossing by C. neoformans. Together with our previous systematic studies of transcription factors and kinases, our results provide comprehensive insight into the pathobiological signalling circuitry of C. neoformans. Phosphatases are key components in cellular signalling networks. Here, the authors present a systematic functional analysis of phosphatases of the fungal pathogen Cryptococcus neoformans, revealing roles in virulence, stress responses, O-mannosylation, retromer function and other processes. English Nature Publishing Group Genome-wide functional analysis of phosphatases in the pathogenic fungus Cryptococcus neoformans Article 10.1038/s41467-020-18028-0 1 Nature Communications, v.11, no.1 Nature Communications 11 1 Y scie scopus 000568890700002 2-s2.0-85089751143 Multidisciplinary Sciences Science & Technology - Other Topics Article CELL-WALL INTEGRITY PROTEIN PHOSPHATASE CANDIDA-ALBICANS SACCHAROMYCES-CEREVISIAE TREHALOSE-6-PHOSPHATE PHOSPHATASE GUANOSINE DIPHOSPHATASE CATALYTIC SUBUNIT ADENYLYL-CYCLASE CONTROLS GROWTH HYPHAL GROWTH