These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Oligomerization of SCFTIR1 Is Essential for Aux/IAA Degradation and Auxin Signaling in Arabidopsis. Author: Dezfulian MH, Jalili E, Roberto DK, Moss BL, Khoo K, Nemhauser JL, Crosby WL. Journal: PLoS Genet; 2016 Sep; 12(9):e1006301. PubMed ID: 27618443. Abstract: The phytohormone auxin is a key regulator of plant growth and development. Molecular studies in Arabidopsis have shown that auxin perception and signaling is mediated via TIR1/AFB-Aux/IAA co-receptors that assemble as part of the SCFTIR1/AFB E3 ubiquitin-ligase complex and direct the auxin-regulated degradation of Aux/IAA transcriptional repressors. Despite the importance of auxin signaling, little is known about the functional regulation of the TIR1/AFB receptor family. Here we show that TIR1 can oligomerize in planta via a set of spatially clustered amino acid residues. While none of the residues identified reside in the interaction interface of the TIR1-Aux/IAA degron, they nonetheless regulate the binding of TIR1 to Aux/IAA substrate proteins and their subsequent degradation in vivo as an essential aspect of auxin signaling. We propose oligomerization of TIR1 as a novel regulatory mechanism in the regulation of auxin-mediated plant patterning and development.[Abstract] [Full Text] [Related] [New Search]