The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit

• Main Authors: Yong, J.Y.A, Wang, Y.-M, Wang, Y
• Other Authors: DEPT OF BIOCHEMISTRY
• Format: Article
• Published: Company of Biologists Ltd 2020
• Subjects: phospholipid; phosphoprotein phosphatase Cdc14; protein Gin4; protein kinase; protein Nim1; septin; unclassified drug; fungal protein; protein binding; Article; Candida albicans; cell cycle regulation; cell membrane; controlled study; enzyme substrate; lipid binding domain; mitosis; mutant; nonhuman; nucleolus; nucleolus associating domain; priority journal; protein assembly; protein dephosphorylation; protein domain; protein function; protein protein interaction; septin binding domain; yeast cell; biological model; chemistry; cytology; enzymology; metabolism; phosphorylation; protein transport; Cell Membrane; Cell Nucleolus; Fungal Proteins; Mitosis; Models, Biological; Phospholipids; Phosphorylation; Protein Binding; Protein Domains; Protein Transport; Septins
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/179297
• Institution: National University of Singapore

10.1242/jcs.183160