Phosphorylation of intrinsically disordered regions in remorin proteins

Marin, Macarena; Ott, Thomas (2012): Phosphorylation of intrinsically disordered regions in remorin proteins. In: Frontiers in Plant Science, Vol. 3, 86

Abstract

Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signaling proteins such as receptor-like kinases 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.

• Item Type: Journal article
• Form of publication: Publisher's Version
• Keywords: remorin; phosphorylation; intrinsic disorder; signaling
• Faculties: Biology > Department Biology I
• Subjects: 500 Science > 570 Life sciences; biology
• ISSN: 1664-462X
• Place of Publication: PO BOX 110, LAUSANNE, 1015, SWITZERLAND
• Language: English