The single‐subunit RING‐type E3 ubiquitin ligase RSL1 targets PYL4 and PYR1 ABA receptors in plasma membrane to modulate abscisic acid signaling

• DOI: 10.1111/tpj.12708
• Publication Date: 2014-10-20T13:44:07Z
• Authors: Eduardo Bueso; Lesia Rodriguez; Laura Lorenzo‐Orts; Miguel Gonzalez‐G...; Enric Sayas; Jesús Muñoz‐Bertomeu; Carla Ibañez; Ramón Serrano; Pedro L. Rodriguez
• Keywords: 0301 basic medicine; Protein turnover; RFA gene family; ABA receptor; Arabidopsis thaliana; Arabidopsis Proteins; Ubiquitin-Protein Ligases; Cell Membrane; Arabidopsis; Ubiquitination; Membrane Transport Proteins; MICROBIOLOGIA; Receptors, Cell Surface; 03 medical and health sciences; Gene Expression Regulation, Plant; BIOQUIMICA Y BIOLOGIA MOLECULAR; Basic Helix-Loop-Helix Transcription Factors; RING E3 ubiquitin ligase; Abscisic Acid; Half-Life; Signal Transduction

Membrane-delimited events play a crucial role for ABA signaling and PYR/PYL/RCAR receptors, clade A PP2Cs SnRK2/CPK kinases modulate the activity of different plasma membrane components involved in action. Therefore, turnover PYR/PYL/RCARs proximity might be step that affects receptor function downstream signaling. In this study we describe single-subunit RING-type E3 ubiquitin ligase RSL1 interacts with PYL4 PYR1 receptors at membrane. Overexpression reduces sensitivity rsl1 RNAi lines impair expression several members RSL1/RFA gene family show enhanced to ABA. bears C-terminal transmembrane domain targets Accordingly, bimolecular fluorescent complementation (BiFC) studies showed RSL1-PYL4 RSL1-PYR1 interaction is localized promoted degradation vivo mediated vitro ubiquitylation receptors. Taken together, these results suggest process affect their via effect on half-life, protein interactions or trafficking.