Details

Autor(en) / Beteiligte

• Dezfulian, Mohammad H
• Jalili, Espanta
• Roberto, Don Karl A
• Moss, Britney L
• Khoo, Kerry
• Nemhauser, Jennifer L
• Crosby, William L
• Yu, Hao

Titel

Oligomerization of SCFTIR1 Is Essential for Aux/IAA Degradation and Auxin Signaling in Arabidopsis

Ist Teil von

• PLoS genetics, 2016-09, Vol.12 (9), p.e1006301-e1006301

Ort / Verlag

United States: Public Library of Science

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.