Shugoshin ensures maintenance of the spindle assembly checkpoint response and efficient spindle disassembly
Autor: | Aakanksha Sane, Shreyas Sridhar, Kaustuv Sanyal, Santanu K. Ghosh |
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Rok vydání: | 2021 |
Předmět: |
Mad2
Condensin Spindle disassembly BUB1 Mitosis Cell Cycle Proteins Spindle Apparatus Chromatids Protein Serine-Threonine Kinases Microbiology Genomic Instability Fungal Proteins Chromosome Segregation Candida albicans Humans Kinetochores Molecular Biology Adenosine Triphosphatases Sister chromatid biorientation biology Kinetochore Candidiasis Nuclear Proteins Cell biology Spindle apparatus DNA-Binding Proteins Spindle checkpoint Multiprotein Complexes biology.protein M Phase Cell Cycle Checkpoints |
Zdroj: | Molecular Microbiology. 116:1079-1098 |
ISSN: | 1365-2958 0950-382X |
DOI: | 10.1111/mmi.14796 |
Popis: | Shugoshin proteins are evolutionarily conserved across eukaryotes, with some species-specific cellular functions, ensuring the fidelity of chromosome segregation. They act as adaptors at various subcellular locales to mediate several protein-protein interactions in a spatio-temporal manner. Here, we characterize shugoshin (Sgo1) in the human fungal pathogen Candida albicans. We observe that Sgo1 retains its centromeric localization and performs its conserved functions of regulating the sister chromatid biorientation, centromeric condensin localization, and maintenance of chromosomal passenger complex (CPC). We identify novel roles of Sgo1 as a spindle assembly checkpoint (SAC) component with functions in maintaining a prolonged SAC response by retaining Mad2 and Bub1 at the kinetochores in response to improper kinetochore-microtubule attachments. Strikingly, we discover the in vivo localization of Sgo1 along the length of the mitotic spindle. Our results indicate that Sgo1 performs a hitherto unknown function of facilitating timely disassembly of the mitotic spindle in C. albicans. To summarize, this study unravels a unique functional adaptation of shugoshin in maintaining genomic stability. |
Databáze: | OpenAIRE |
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