A subcellular map of the human kinome

The human kinome comprises 538 kinases playing essential functions by catalyzing protein phosphorylation. Annotation of subcellular distribution of the kinome greatly facilitates investigation of normal and disease mechanisms. Here, we present Kinome Atlas (KA), an image-based map of the kinome anno...

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Published ineLife Vol. 10
Main Authors Zhang, Haitao, Cao, Xiaolei, Tang, Mei, Zhong, Guoxuan, Si, Yuan, Li, Haidong, Zhu, Feifeng, Liao, Qinghua, Li, Liuju, Zhao, Jianhui, Feng, Jia, Li, Shuaifeng, Wang, Chenliang, Kaulich, Manuel, Wang, Fangwei, Chen, Liangyi, Li, Li, Xia, Zongping, Liang, Tingbo, Lu, Huasong, Feng, Xin-Hua, Zhao, Bin
Format Journal Article
LanguageEnglish
Published England eLife Science Publications, Ltd 14.05.2021
eLife Sciences Publications Ltd
eLife Sciences Publications, Ltd
Subjects
Antibodies
Antigenic determinants
Biochemistry and Chemical Biology
Cell Biology
Cloning
Cristae
Epitopes
Experiments
Kinases
kinome
Localization
Mitochondria
mitochondrial
MOK
Oxidative stress
phase separation
Phosphorylation
Plasma
Plasmids
Proteins
subcellular localization
Tools and Resources
cell biology
chemical biology
human
biochemistry
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Summary:The human kinome comprises 538 kinases playing essential functions by catalyzing protein phosphorylation. Annotation of subcellular distribution of the kinome greatly facilitates investigation of normal and disease mechanisms. Here, we present Kinome Atlas (KA), an image-based map of the kinome annotated to 10 cellular compartments. 456 epitope-tagged kinases, representing 85% of the human kinome, were expressed in HeLa cells and imaged by immunofluorescent microscopy under a similar condition. KA revealed kinase family-enriched subcellular localizations and discovered a collection of new kinase localizations at mitochondria, plasma membrane, extracellular space, and other structures. Furthermore, KA demonstrated the role of liquid-liquid phase separation in formation of kinase condensates. Identification of MOK as a mitochondrial kinase revealed its function in cristae dynamics, respiration, and oxidative stress response. Although limited by possible mislocalization due to overexpression or epitope tagging, this subcellular map of the kinome can be used to refine regulatory mechanisms involving protein phosphorylation.
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ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.64943