Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis
Yi Zhang,
Nino Nikolovski,
Mathias Sorieul,
Tamara Vellosillo,
Heather E. McFarlane,
Ray Dupree,
Christopher Kesten,
René Schneider,
Carlos Driemeier,
Rahul Lathe,
Edwin Lampugnani,
Xiaolan Yu,
Alexander Ivakov,
Monika S. Doblin,
Jenny C. Mortimer,
Steven P. Brown,
Staffan Persson () and
Paul Dupree ()
Additional contact information
Yi Zhang: Max-Planck Institute for Molecular Plant Physiology
Nino Nikolovski: University of Cambridge
Mathias Sorieul: University of Cambridge
Tamara Vellosillo: Energy Biosciences Institute, University of California
Heather E. McFarlane: School of Biosciences, University of Melbourne
Ray Dupree: University of Warwick
Christopher Kesten: School of Biosciences, University of Melbourne
René Schneider: School of Biosciences, University of Melbourne
Carlos Driemeier: Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)
Rahul Lathe: Max-Planck Institute for Molecular Plant Physiology
Edwin Lampugnani: School of Biosciences, University of Melbourne
Xiaolan Yu: University of Cambridge
Alexander Ivakov: School of Biosciences, University of Melbourne
Monika S. Doblin: School of Biosciences, University of Melbourne
Jenny C. Mortimer: University of Cambridge
Steven P. Brown: University of Warwick
Staffan Persson: Max-Planck Institute for Molecular Plant Physiology
Paul Dupree: University of Cambridge
Nature Communications, 2016, vol. 7, issue 1, 1-14
Abstract:
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 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.
Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11656
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DOI: 10.1038/ncomms11656
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