A suite of fluorescent timers for visualizing protein spatiotemporal dynamics in plants

Fluorescent timers (FTs), including tandem FTs (tdFTs), enable real-time visualization of precise protein localization and turnover within living cells, an essential property for elucidating protein function. In plants, application of FT has been limited largely because of the mismatch between FT maturation kinetics and the slow growth rate of plant cells. Here, we systematically evaluated multiple FT configurations to identify tdFTs optimized for plant systems. Using Arabidopsis thaliana , we tested a range of fluorescent proteins (FPs) differing in maturation times. Functional tdFT expression was confirmed in diverse organelles. Selected tdFT configurations were developed to track protein biogenesis/turnover in autoimmunity, protein transport in abiotic stress, and polarized protein translocation in determination of cell fate. When the large size of tdFT interfered with protein mobility, we developed a bipartite FT, separately tagging proteins with different FPs. This resource provides a framework for selecting FTs to dissect dynamic protein behaviors in plant cells.

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Publication Details

Journal
Science Advances
Published
2026-09-16
DOI
https://doi.org/10.1126/sciadv.aef3538
Primary Topic
Plant Molecular Biology Research
Type
article
Field-Weighted Citation Impact
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article

A suite of fluorescent timers for visualizing protein spatiotemporal dynamics in plants

Suji Ye, Xue Ding, Libo Shan, Hisashi Koiwa et al.
Science Advances
Plant Molecular Biology Research
article

A suite of fluorescent timers for visualizing protein spatiotemporal dynamics in plants

Suji Ye, Xue Ding, Libo Shan, Hisashi Koiwa, Yukihiro Nagashima, Juan Dong, Fausto Andres Ortiz‐Morea, Xin Qiao, Jun Liu, Vinita Sharma, Derui Liu, Qiaochu Shen
article en

Abstract

Fluorescent timers (FTs), including tandem FTs (tdFTs), enable real-time visualization of precise protein localization and turnover within living cells, an essential property for elucidating protein function. In plants, application of FT has been limited largely because of the mismatch between FT maturation kinetics and the slow growth rate of plant cells. Here, we systematically evaluated multiple FT configurations to identify tdFTs optimized for plant systems. Using Arabidopsis thaliana , we tested a range of fluorescent proteins (FPs) differing in maturation times. Functional tdFT expression was confirmed in diverse organelles. Selected tdFT configurations were developed to track protein biogenesis/turnover in autoimmunity, protein transport in abiotic stress, and polarized protein translocation in determination of cell fate. When the large size of tdFT interfered with protein mobility, we developed a bipartite FT, separately tagging proteins with different FPs. This resource provides a framework for selecting FTs to dissect dynamic protein behaviors in plant cells.

Science AdvancesVol. 12(38)
Rutgers, The State University of New Jersey (US), University of Michigan (US), Texas A&M University (US)
Openalex Percentile: Top 12%
Plant Molecular Biology Research
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