Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins

Frontiers in Plant Science. 2012;3 DOI 10.3389/fpls.2012.00086


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Journal Title: Frontiers in Plant Science

ISSN: 1664-462X (Online)

Publisher: Frontiers Media S.A.

LCC Subject Category: Agriculture: Plant culture

Country of publisher: Switzerland

Language of fulltext: English

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Macarena eMarín (University of Munich (LMU))
Thomas eOtt (University of Munich (LMU))


Blind peer review

Editorial Board

Instructions for authors

Time From Submission to Publication: 14 weeks


Abstract | Full Text

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.