한빛사논문
- 조회633
Tae-Wuk Kim1,2,3,† Chan Ho Park1,†, Chuan-Chih Hsu1,4,†, Yeong-Woo Kim2, Yeong-Woo Ko2, Zhenzhen Zhang1, Jia-Ying Zhu1, Yu-Chun Hsiao1, Tess Branon5,6,7, Krista Kaasik8, Evan Saldivar1,6, Kevin Li1, Asher Pasha9, Nicholas J. Provart9, Alma L. Burlingame8, Shou-Ling Xu1, Alice Y. Ting5,6,10 and Zhi-Yong Wang1,*
1 Department of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA
2 Department of Life Science, Hanyang University, Seoul 04763, South Korea
3 Research Institute for Convergence of Basic Science, Hanyang University, Seoul 04763, South Korea
4 Institute of Plant and Microbial Biology, Academia Sinica, Taipei 11529, Taiwan
5 Departments of Genetics, Biology, and Chemistry, Stanford University, Stanford, California 94305, USA
6 Department of Biology, Stanford University, Stanford, California 94305, USA
7 Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
8 Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA
9Departmentof Cell & Systems Biology/Centre for the Analysis of Genome Evolution and Function, University of Toronto,Toronto, Ontario M5S 3B2, Canada
10Chan Zuckerberg Biohub, San Francisco, California, USA
*Author for correspondence: Zhi-Yong Wang
†T.-W.K., C.H.P., and C.-C.H. contributed equally to this work.
Abstract
Elucidating enzyme-substrate relationships in posttranslational modification (PTM) networks is crucial for understanding signal transduction pathways but is technically difficult because enzyme-substrate interactions tend to be transient. Here we demonstrate that TurboID-based proximity labeling (TbPL) effectively and specifically captures the substrates of kinases and phosphatases. TbPL-mass spectrometry (TbPL-MS) identified over four hundred proximal proteins of Arabidopsis thaliana BRASSINOSTEROID-INSENSITIVE2 (BIN2), a member of the GLYCOGEN SYNTHASE KINASE 3 (GSK3) family that integrates signaling pathways controlling diverse developmental and acclimation processes. A large portion of the BIN2 proximal proteins showed BIN2-dependent phosphorylation in vivo or in vitro, suggesting that these are BIN2 substrates. Protein-protein interaction network analysis showed that the BIN2 proximal proteins include interactors of BIN2 substrates, revealing a high level of interactions among the BIN2 proximal proteins. Our proteomic analysis establishes the BIN2 signaling network and uncovers BIN2 functions in regulating key cellular processes such as transcription, RNA processing, translation initiation, vesicle trafficking, and cytoskeleton organization. We further discovered significant overlap between the GSK3 phosphorylome and the O-GlcNAcylome, suggesting an evolutionarily ancient relationship between GSK3 and the nutrient-sensing O-glycosylation pathway. Our work presents a powerful method for mapping PTM networks, a large dataset of GSK3 kinase substrates, and important insights into the signaling network that controls key cellular functions underlying plant growth and acclimation.
논문정보
- Research article
- 2023년 01월 (BRIC 등록일 2023-03-08)
- 국내+국외 연구진
- 생명과학 > 식물학
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