The Companion of Cellulose Synthase 1 confers salt tolerance through a Tau-like mechanism in plants

Microtubules arefilamentous structures necessary for cell division, motility and morphology,with dynamics critically regulated by microtubule-associated proteins (MAPs). Here weoutline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYN-THASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth undersalt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules atevenly distributed points through four conserved hydrophobic regions. By NMR and live cellanalyses we reveal that two neighboring residues in thefirst hydrophobic binding motif arecrucial for the microtubule interaction. The microtubule-binding mechanism of CC1 isreminiscent to that of the prominent neuropathology-related protein Tau, indicating evolu-tionary convergence of MAP functions across animal and plant cells.
Nature Communications, 10 (1)
ISSN:2041-1723