Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins

• Main Authors: Macarena eMarín, Thomas eOtt
• Format: Article
• Language: English
• Published: Frontiers Media S.A. 2012-05-01
• Series: Frontiers in Plant Science
• Subjects: Phosphorylation; remorin; intrinsic disorder; signalling
• Online Access: http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00086/full

Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signalling proteins such as receptor-like kinases (RLKs) and may dynamically modulate their lateral segregation within plasma membranes. Recent evidence suggests such functions of remorins during plant-microbe interactions and innate immune responses, where differential phosphorylation of some of these proteins has been described to be dependent on the perception of the microbe-associated molecular pattern (MAMP) flg22 and the presence of the NBS-LRR resistance protein RPM1. A number of specifically phosphorylated residues in their highly variable and intrinsically disordered N-terminal regions have been identified. Sequence diversity of these evolutionary distinct domains suggests that remorins may serve a wide range of biological functions. Here, we describe patterns and features of intrinsic disorder in remorin protein and discuss possible functional implications of phosphorylation within these rapidly evolving domains.