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https://doi.org/10.1101/090563...
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http://genesdev.cshlp.org/cont...
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Genes & Development
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PubMed Central
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Genes & Development
Article . 2017 . Peer-reviewed
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Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis

Authors: Dong, Hui; Dumenil, Jack; Lu, Fu-Hao; Na, Li; Vanhaeren, Hannes; Naumann, Christin; Klecker, Maria; +12 Authors

Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis

Abstract

ABSTRACTThe characteristic shapes and sizes of organs are established by cell proliferation patterns and final cell sizes, but the underlying molecular mechanisms coordinating these are poorly understood. Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell proliferation during organ growth inArabidopsis thaliana. The peptidase is activated by two RING E3 ligases, BB and DA2, which are subsequently cleaved by the activated peptidase and destabilized. In the case of BB, cleavage leads to destabilization by the RING E3 ligase PRT1 of the N-end rule pathway. DA1 peptidase activity also cleaves the de-ubiquitylase UBP15, which promotes cell proliferation, and the transcription factors TCP15 and TCP22, which promote cell proliferation proliferation and repress endoreduplication. We propose that DA1 peptidase activity regulates the duration of cell proliferation and the transition to endoreduplication and differentiation during organ formation in plants by coordinating the destabilization of regulatory proteins.

Country
Belgium
Keywords

N-end rule-mediated degradation, Ubiquitin-Protein Ligases, Arabidopsis, GENE FAMILY, DA1, END RULE PATHWAY, UBIQUITIN-BINDING PROTEINS, CYCLE, ubiquitylation, Cell Proliferation, THALIANA, ORGAN SIZE, Arabidopsis Proteins, Protein Stability, Ubiquitination, Biology and Life Sciences, organ size, LIM Domain Proteins, ubiquitin-activated peptidase, LEAF DEVELOPMENT, BIG BROTHER, Enzyme Activation, COUPLED MONOUBIQUITINATION, Research Paper

  • BIP!
    Impact byBIP!
    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    137
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 1%
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Top 1%
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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
137
Top 1%
Top 10%
Top 1%
Green
Published in a Diamond OA journal