The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA.

dc.contributor.author

Zentella, Rodolfo

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Sui, Ning

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Barnhill, Benjamin

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Hsieh, Wen-Ping

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Hu, Jianhong

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Shabanowitz, Jeffrey

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Boyce, Michael

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Olszewski, Neil E

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Zhou, Pei

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Hunt, Donald F

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Sun, Tai-Ping

dc.coverage.spatial

United States

dc.date.accessioned

2017-12-01T18:33:52Z

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2017-12-01T18:33:52Z

dc.date.issued

2017-05

dc.description.abstract

Plant development requires coordination among complex signaling networks to enhance the plant's adaptation to changing environments. DELLAs, transcription regulators originally identified as repressors of phytohormone gibberellin signaling, play a central role in integrating multiple signaling activities via direct protein interactions with key transcription factors. Here, we found that DELLA is mono-O-fucosylated by the novel O-fucosyltransferase SPINDLY (SPY) in Arabidopsis thaliana. O-fucosylation activates DELLA by promoting its interaction with key regulators in brassinosteroid- and light-signaling pathways, including BRASSINAZOLE-RESISTANT1 (BZR1), PHYTOCHROME-INTERACTING-FACTOR3 (PIF3) and PIF4. Moreover, spy mutants displayed elevated responses to gibberellin and brassinosteroid, and increased expression of common target genes of DELLAs, BZR1 and PIFs. Our study revealed that SPY-dependent protein O-fucosylation plays a key role in regulating plant development. This finding may have broader importance because SPY orthologs are conserved in prokaryotes and eukaryotes, thus suggesting that intracellular O-fucosylation may regulate a wide range of biological processes in diverse organisms.

dc.identifier

https://www.ncbi.nlm.nih.gov/pubmed/28244988

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nchembio.2320

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1552-4469

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https://hdl.handle.net/10161/15816

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eng

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Springer Science and Business Media LLC

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Nat Chem Biol

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10.1038/nchembio.2320

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Arabidopsis

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Arabidopsis Proteins

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Fucosyltransferases

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Repressor Proteins

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The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA.

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Journal article

duke.contributor.orcid

Boyce, Michael|0000-0002-2729-4876

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Zhou, Pei|0000-0002-7823-3416

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Sun, Tai-Ping|0000-0001-5223-2936

pubs.author-url

https://www.ncbi.nlm.nih.gov/pubmed/28244988

pubs.begin-page

479

pubs.end-page

485

pubs.issue

5

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Basic Science Departments

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Biochemistry

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Biology

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Chemistry

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Duke

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Duke Cancer Institute

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Institutes and Centers

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School of Medicine

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Temp group - logins allowed

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Trinity College of Arts & Sciences

pubs.publication-status

Published

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13

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