F1000 recommends a recent paper from the Ott lab (Marín et al., 2012) as being of special significance in the field.
The recent paper Marín et al. (published by the lab of Thomas Ott in December 2012) that reported on intrinsic disorder in the remorin protein AtREM1.3 has been recommended in Faculty of 1000.
Marín M, Thallmair V and Ott T (2012)
The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions
Journal of Biological Chemistry, 287: 39982-39991
The longstanding structure-function paradigm, which states that a protein only serves a biological function in a structured state, had to be substantially revised with the description of intrinsic disorder in proteins. Intrinsically disordered regions that undergo a stimulus-dependent disorder-to-order transition are common to a large number of signaling proteins. However, little is known about the functionality of intrinsically disordered regions in plant proteins. Here we investigated intrinsic disorder in a plant-specific remorin protein that has been described as a signaling component in plant-microbe interactions. Using bioinformatic, biochemical, and biophysical approaches, we characterized the highly abundant remorin AtREM1.3, showing that its N-terminal region is intrinsically disordered. Although only the AtREM1.3 C-terminal domain is essential for stable homo-oligomerization, the N-terminal region facilitates this interaction. Furthermore, we confirmed the stable interaction between AtREM1.3 and four isoforms of the importin α protein family in a yeast two-hybrid system and by an in planta bimolecular fluorescent complementation assay. Phosphorylation of Ser-66 in the intrinsically disordered N-terminal region decreases the interaction strength with the importin α proteins. Hence, the N-terminal region may constitute a regulatory domain, stabilizing these interactions.