Journal article
Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis
Y Zhang, N Nikolovski, M Sorieul, T Vellosillo, HE McFarlane, R Dupree, C Kesten, R Schneider, C Driemeier, R Lathe, E Lampugnani, X Yu, A Ivakov, MS Doblin, JC Mortimer, SP Brown, S Persson, P Dupree
Nature Communications | NATURE PUBLISHING GROUP | Published : 2016
DOI: 10.1038/ncomms11656
Abstract
As the most abundant biopolymer on Earth, cellulose is a key structural component of the plant cell wall. Cellulose is produced at the plasma membrane by cellulose synthase (CesA) complexes (CSCs), which are assembled in the endomembrane system and trafficked to the plasma membrane. While several proteins that affect CesA activity have been identified, components that regulate CSC assembly and trafficking remain unknown. Here we show that STELLO1 and 2 are Golgi-localized proteins that can interact with CesAs and control cellulose quantity. In the absence of STELLO function, the spatial distribution within the Golgi, secretion and activity of the CSCs are impaired indicating a central role o..
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Awarded by European Commission
Funding Acknowledgements
The work presented in this paper was supported by grants from the BBSRC: BB/G016240/1 BBSRC Sustainable Energy Centre Cell Wall Sugars Programme (BSBEC) and the European Community's Seventh Framework Programme SUNLIBB (FP7/2007-2013) under the grant agreement no. 251132 to P.D. The UK 850MHz solid-state NMR facility was funded by EPSRC and BBSRC, as well as the University of Warwick including via part funding through Birmingham Science City Advanced Materials Projects 1 and 2 supported by Advantage West Midlands (AWM) and the European Regional Development Fund (ERDF); we thank Dinu Iuga for experimental assistance, Luisa Trindade for providing split-ubiquitin constructs, and Chris Somerville for helpful discussions and suggesting the name STELLO. We acknowledge LNBio and LNLS for providing X-ray beam time (proposal GAR 15208), and the Sainsbury Laboratory Cambridge University for imaging facilities. T.V. was supported by an EMBO long-term fellowship (ALTF 711-2012) and by postdoctoral funding from the Philomathia Foundation. H.E.M. was supported by an EMBO Long-Term Fellowship (ALTF-1246-2013) and an NSERC Postdoctoral Fellowship (PDF-454454-2014). S.P. and Y.Z. were supported by the Max-Planck Gesellschaft, and S.P. was also supported by a R@MAP Professor position at UoM. We thank the Biological Optical Microscopy Platform (BOMP) at University of Melbourne, and Tom Simmons and Rita Marques for assistance on sugar analyses.