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

10.1242/jcs.183160

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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
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1792972023-10-31T22:10:15Z The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit Yong, J.Y.A Wang, Y.-M Wang, Y DEPT OF BIOCHEMISTRY phospholipid phosphoprotein phosphatase Cdc14 protein Gin4 protein kinase protein Nim1 septin unclassified drug fungal protein phospholipid protein binding septin 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 domain protein transport Candida albicans Cell Membrane Cell Nucleolus Fungal Proteins Mitosis Models, Biological Phospholipids Phosphorylation Protein Binding Protein Domains Protein Transport Septins 10.1242/jcs.183160 Journal of Cell Science 129 14 2744-2756 2020-10-23T02:46:33Z 2020-10-23T02:46:33Z 2016 Article Yong, J.Y.A, Wang, Y.-M, Wang, Y (2016). The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit. Journal of Cell Science 129 (14) : 2744-2756. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.183160 0021-9533 https://scholarbank.nus.edu.sg/handle/10635/179297 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Company of Biologists Ltd Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	phospholipid phosphoprotein phosphatase Cdc14 protein Gin4 protein kinase protein Nim1 septin unclassified drug fungal protein phospholipid protein binding septin 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 domain protein transport Candida albicans Cell Membrane Cell Nucleolus Fungal Proteins Mitosis Models, Biological Phospholipids Phosphorylation Protein Binding Protein Domains Protein Transport Septins
spellingShingle	phospholipid phosphoprotein phosphatase Cdc14 protein Gin4 protein kinase protein Nim1 septin unclassified drug fungal protein phospholipid protein binding septin 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 domain protein transport Candida albicans Cell Membrane Cell Nucleolus Fungal Proteins Mitosis Models, Biological Phospholipids Phosphorylation Protein Binding Protein Domains Protein Transport Septins Yong, J.Y.A Wang, Y.-M Wang, Y The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
description	10.1242/jcs.183160
author2	DEPT OF BIOCHEMISTRY
author_facet	DEPT OF BIOCHEMISTRY Yong, J.Y.A Wang, Y.-M Wang, Y
format	Article
author	Yong, J.Y.A Wang, Y.-M Wang, Y
author_sort	Yong, J.Y.A
title	The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
title_short	The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
title_full	The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
title_fullStr	The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
title_full_unstemmed	The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
title_sort	nim1 kinase gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit
publisher	Company of Biologists Ltd
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/179297
_version_	1781792336834985984

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

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