Journal
MOLECULAR CELL
Volume 76, Issue 1, Pages 177-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2019.06.044
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Funding
- William H. Danforth Plant Science Fellowship Program
- National Science Foundation [IOS-1453750, MCB-1453130, MCB-1614539, MCB-1614766]
- NIH [R01 GM112898-01, R01 5NS056114]
- National Research Foundation of Korea [2017R1A2A1A17069734]
- NSF Center for Engineering Mechanobiology [CMMI-1548571]
- St. Jude Research Collaborative Fund
- USDA-NIFA [MOW-2014-01877]
- NCI Cancer Center [P30 CA91842]
- ICTS/CTSA from the National Center for Research Resources (NCRR), a component of the NIH [UL1TR000448]
- NIH Roadmap for Medical Research
- National Research Foundation of Korea [2017R1A2A1A17069734] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The phytohormone auxin plays crucial roles in nearly every aspect of plant growth and development. The auxin response factor (ARF) transcription factor family regulates auxin-responsive gene expression and exhibits nuclear localization in regions of high auxin responsiveness. Here we show that the ARF7 and ARF19 proteins accumulate in micron-sized assemblies within the cytoplasm of tissues with attenuated auxin responsiveness. We found that the intrinsically disordered middle region and the folded PB1 interaction domain of ARFs drive protein assembly formation. Mutation of a single lysine within the PB1 domain abrogates cytoplasmic assemblies, promotes ARF nuclear localization, and results in an altered transcriptome and morphological defects. Our data suggest a model in which ARF nucleo-cyto-plasmic partitioning regulates auxin responsiveness, providing a mechanism for cellular competence for auxin signaling.
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