ArticleJournal of cell science2016
The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Exploring fungal survival mechanisms: toward next-generation antifungal therapies against Candida spp.Archives of microbiology · 2025Review
- Cdc14 phosphatase contributes to cell wall integrity and pathogenesis inFrontiers in microbiology · 2023Article
- Septins as membrane influencers: direct play or in association with other cytoskeleton partners.Frontiers in cell and developmental biology · 2023Review
- Lipid Polarization during Cytokinesis.Cells · 2022Review
- From Jekyll to Hyde: The Yeast-Hyphal Transition ofPathogens (Basel, Switzerland) · 2021Review
- Proteins that physically interact with the phosphatase Cdc14 in Candida albicans have diverse roles in the cell cycle.Scientific reports · 2019Article
- Protein-Protein Interactions inFrontiers in microbiology · 2019Review
- Effect of Nicotinamide AgainstFrontiers in microbiology · 2019Article
- Septin localization and function during autophagy.Current genetics · 2018Review
- Forging the ring: from fungal septins' divergent roles in morphology, septation and virulence to factors contributing to their assembly into higher order structures.Microbiology (Reading, England) · 2016Review
- Septin Organization and Functions in Budding Yeast.Frontiers in cell and developmental biology · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In fungi, the Nim1 protein kinases, such as Gin4, are important regulators of multiple cell cycle events, including the G2-M transition, septin assembly, polarized growth and cytokinesis. Compelling evidence has linked some key functions of Gin4 with the large C-terminal non-kinase region which, however, is poorly defined. By systematically dissecting and functionally characterizing the non-kinase region of Gin4 in the human fungal pathogen Candida albicans, we report the identification of three new domains with distinct functions: a lipid-binding domain (LBD), a septin-binding domain (SBD) and a nucleolus-associating domain (NAD). The LBD and SBD are indispensable for the function of Gin4, and they alone could sufficiently restore septin ring assembly in GIN4-null mutants. The NAD localizes to the periphery of the nucleolus and physically associates with Cdc14, the ultimate effector of the mitotic exit network. Gin4 mutants that lack the NAD are defective in spindle orientation and exit mitosis prematurely. Furthermore, we show that Gin4 is a substrate of Cdc14. These findings provide novel insights into the roles and mechanisms of Nim1 kinases in the regulation of some crucial cell cycle events.
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