Auxin-induced SCFTIR1–Aux/IAA interaction involves stable modification of the SCFTIR1 complex
AUTOR(ES)
Kepinski, Stefan
FONTE
National Academy of Sciences
RESUMO
The plant hormone auxin can regulate gene expression by destabilizing members of the Aux/IAA family of transcriptional repressors. Auxin-induced Aux/IAA degradation requires the protein-ubiquitin ligase SCFTIR1, with auxin acting to enhance the interaction between the Aux/IAAs and SCFTIR1. SKP1, Cullin, and an F-box-containing protein (SCF)-mediated degradation is an important component of many eukaryotic signaling pathways. In all known cases to date, the interaction between the targets and their cognate SCFs is regulated by signal-induced modification of the target. The mechanism by which auxin promotes the interaction between SCFTIR1 and Aux/IAAs is not understood, but current hypotheses propose auxin-induced phosphorylation, hydroxylation, or proline isomerization of the Aux/IAAs. We found no evidence to support these hypotheses or indeed that auxin induces any stable modification of Aux/IAAs to increase their affinity for SCFTIR1. Instead, we present data suggesting that auxin promotes the SCFTIR1–Aux/IAA interaction by affecting the SCF component, TIR1, or proteins tightly associated with it.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=514484Documentos Relacionados
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