Fig. 6
From: The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
Cartoon overview of the CC1-microtubule interaction and its similarity to Tau despite sequential differences. a Cartoon representation of the CC1 and hTau40 domain architecture. CC1 is composed of a cytosolic N-Terminus, transmembrane domain (TM) and an apoplastic C-terminal domain. hTau40 represents the longest isoform in humans containing two N-terminal inserts (I1, I2) in the projection domain, a polyproline region (PRR) and four imperfect repeats (R1–R4) in the microtubule assembly region (MTAR). The position of the four respective microtubule-binding regions are marked and highlighted green in CC1. The amino acid sequences below compare the NMR-derived microtubule-binding regions of CC1 and Tau. Identical (green) and similar (orange; score of ≥0 in the BLOSUM62 matrix) amino acids are highlighted. b CC1 localization in its cellular context as part of the cellulose synthase complex (CSC). While the CSCs migrate along cortical microtubules during cellulose production, CC1 is involved in microtubule array organization via its cytosolic N-terminus. Similar to the Tau binding behavior, the CC1-microtubule interaction is dynamic and the microtubule-binding motifs (green) are potentially able to bind several tubulin dimers, distributed over one or several microtubules, thereby affecting microtubule bundling or dynamics. The individual components of the cartoon representation are drawn to scale, except for CC1 thickness and omission of its apoplastic domain. Membrane association and length of CC1, as well as the microtubule diameter, determine possible interaction modes
