| http://purl.uniprot.org/citations/19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19309453 | http://www.w3.org/2000/01/rdf-schema#comment | "The plant hormone auxin (indole-3-acetic acid or IAA) regulates plant development by inducing rapid cellular responses and changes in gene expression. Auxin promotes the degradation of Aux/IAA transcriptional repressors, thereby allowing auxin response factors (ARFs) to activate the transcription of auxin-responsive genes. Auxin enhances the binding of Aux/IAA proteins to the receptor TIR1, which is an F-box protein that is part of the E3 ubiquitin ligase complex SCF(TIR1). Binding of Aux/IAA proteins leads to degradation via the 26S proteasome, but evidence for SCF(TIR1)-mediated poly-ubiquitination of Aux/IAA proteins is lacking. Here we used an Arabidopsis cell suspension-based protoplast system to find evidence for SCF(TIR1)-mediated ubiquitination of the Aux/IAA proteins SHY2/IAA3 and BDL/IAA12. Each of these proteins showed a distinct abundance and repressor activity when expressed in this cell system. Moreover, the amount of endogenous TIR1 protein appeared to be rate-limiting for a proper auxin response measured by the co-transfected DR5::GUS reporter construct. Co-transfection with 35S::TIR1 led to auxin-dependent degradation, and excess of 35S::TIR1 even led to degradation of Aux/IAAs in the absence of auxin treatment. Expression of the mutant tir1-1 protein or the related F-box protein COI1, which is involved in jasmonate signaling, had no effect on Aux/IAA degradation. Our results show that SHY2/IAA3 and BDL/IAA12 are poly-ubiquitinated and degraded in response to increased auxin or TIR1 levels. In conclusion, our data provide experimental support for the model that SCF(TIR1)-dependent poly-ubiquitination of Aux/IAA proteins marks these proteins for degradation by the 26S proteasome, leading to activation of auxin-responsive gene expression."xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-313x.2009.03854.x"xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/author | "Memelink J."xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/author | "Offringa R."xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/author | "Maraschin F.d.o.s. S."xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/name | "Plant J"xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/pages | "100-109"xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/title | "Auxin-induced, SCF(TIR1)-mediated poly-ubiquitination marks AUX/IAA proteins for degradation."xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://purl.uniprot.org/core/volume | "59"xsd:string |
| http://purl.uniprot.org/citations/19309453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19309453 |
| http://purl.uniprot.org/citations/19309453 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19309453 |
| http://purl.uniprot.org/uniprot/#_A0A178VA54-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_A0A1P8AT43-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_B0FV08-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_F4I5P9-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_O04197-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_Q38822-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_Q38830-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/#_Q570C0-mappedCitation-19309453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/Q38830 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/A0A178VA54 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/Q570C0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19309453 |
| http://purl.uniprot.org/uniprot/B0FV08 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19309453 |