Journal article

The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants

C Kesten, A Wallmann, R Schneider, HE McFarlane, A Diehl, GA Khan, BJ van Rossum, ER Lampugnani, WG Szymanski, N Cremer, P Schmieder, KL Ford, F Seiter, JL Heazlewood, C Sanchez-Rodriguez, H Oschkinat, S Persson

Nature Communications | NATURE PUBLISHING GROUP | Published : 2019

Open access

Abstract

Microtubules are filamentous structures necessary for cell division, motility and morphology, with dynamics critically regulated by microtubule-associated proteins (MAPs). Here we outline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYNTHASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth under salt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules at evenly distributed points through four conserved hydrophobic regions. By NMR and live cell analyses we reveal that two neighboring residues in the first hydrophobic binding motif are crucial for the microtubule interaction. The microtubule-binding mechanism of CC1 ..

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Grants

Awarded by Association pour la Recherche sur le Cancer


Funding Acknowledgements

Live cell imaging was performed with equipment maintained by the Center for Microscopy and Image Analysis (University of Zurich) and Scientific Center for Optical and Electron Microscopy (ScopeM, ETH Zurich). We thank Martina Leidert and Natalja Erdmann for help with protein expression and purification and Ines Kretschmar for synthesizing the peptides. We thank Dmytro Puchkov for performing the MT quality control by EM and Tim Scholz (Hannover Medical School) for assistance with the microtubule purification protocol. We also thank the Diez group, especially Felix Ruhnow, (B CUBE Center for Molecular Bioengineering, Dresden) for assistance with microtubule imaging and in vitro assays. The helper plasmid pBAD-sigma 32 (I54N) was a gift from Jeffery Kelly<SUP>73</SUP> (Addgene plasmid #59982), pETM11 was kindly supplied by EMBL Protein Production facility (Heidelberg Germany). We thank the Biological Optical Microscopy Platform, the Melbourne Advanced Microscopy Facility, and the Mass Spectrometry and Proteomics Facility (School of Biosciences and Bio21) at the University of Melbourne. S.P. was supported by an ARC Discovery grant (DP190101941), a Hermon-Slade Grant (Persson HSF 15/4) and a Future Fellowship grant (FT160100218). J.L.H. was supported by an ARC Future Fellowship (FT130101165). H.E.M. was supported by an ARC DECRA (DE170100054). C.S.R. and C.K. were supported by ETHZ and a SNF grant (2-77212-15). R.S. received Computational Biology Research Initiative and Early Career Research Grants from the University of Melbourne. C.K. was supported by a Peter und Traudl Engelhorn-Stiftung fellowship.