Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in ArabidopsisReport as inadecuate


Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis


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Publication Date: 2016-06-09

Journal Title: Nature Communications

Publisher: Nature Publishing Group

Volume: 7

Pages: 11656

Language: English

Type: Article

This Version: Version of Record

Metadata: Show full item record

Citation: Zhang, Y., Nikolovski, N., Sorieul, M., Vellosillo, T., McFarlane, H. E., Dupree, R., Kesten, C., et al. (2016). Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis. Nature Communications, 7 11656. https://doi.org/10.1038/ncomms11656

Description: This is the final version of the article. It first appeared from Nature Publishing Group via http://dx.doi.org/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. We report on STELLO1 and 2, Golgi-localized proteins that can interact with the CesAs and that 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 of the STELLO proteins in CSC assembly. Point mutations in the predicted catalytic domains of the STELLO proteins indicate that they are glycosyltransferases facing the Golgi lumen. Hence, we have uncovered proteins that regulate CSC assembly in the plant Golgi apparatus.

Relationships: Cites: https://www.repository.cam.ac.uk/handle/1810/254646

Sponsorship: 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 n° 251132 to PD. The UK 850 MHz 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, and Chris Somerville for helpful discussions and suggesting the name STELLO. The authors acknowledge LNBio and LNLS for providing X-ray beam time (proposal GAR 15208), and the Sainsbury Laboratory Cambridge University for imaging facilities. TV was supported by an EMBO long-term fellowship (ALTF 711-2012) and by postdoctoral funding from the Philomathia Foundation. HEM was supported by an EMBO Long Term Fellowship (ALTF-1246-2013) and an NSERC Postdoctoral Fellowship (PDF-454454-2014). SP and YZ were supported by the Max-Planck Gesellschaft, and SP was also supported by a R[at]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.

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External DOI: https://doi.org/10.1038/ncomms11656

This record's URL: https://www.repository.cam.ac.uk/handle/1810/254641



Rights: Attribution 4.0 International

Licence URL: http://creativecommons.org/licenses/by/4.0/





Author: Zhang, YiNikolovski, NinoSorieul, MathiasVellosillo, TamaraMcFarlane, Heather E.Dupree, RayKesten, ChristopherSchneider, ReneDriem

Source: https://www.repository.cam.ac.uk/handle/1810/254641



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