1. Academic Validation
  2. CESA TRAFFICKING INHIBITOR inhibits cellulose deposition and interferes with the trafficking of cellulose synthase complexes and their associated proteins KORRIGAN1 and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1

CESA TRAFFICKING INHIBITOR inhibits cellulose deposition and interferes with the trafficking of cellulose synthase complexes and their associated proteins KORRIGAN1 and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1

  • Plant Physiol. 2015 Feb;167(2):381-93. doi: 10.1104/pp.114.249003.
Natasha Worden 1 Thomas E Wilkop 1 Victor Esteva Esteve 1 Richard Jeannotte 1 Rahul Lathe 1 Samantha Vernhettes 1 Bart Weimer 1 Glenn Hicks 1 Jose Alonso 1 John Labavitch 1 Staffan Persson 1 David Ehrhardt 1 Georgia Drakakaki 2
Affiliations

Affiliations

  • 1 Departments of Plant Sciences (N.W., T.E.W., V.E.E., J.L., G.D.) and Veterinary Medicine (R.J., B.W.), University of California, Davis, California 95616;Max-Planck-Institute of Molecular Plant Physiology, Science Campus, 14476 Golm, Germany (R.L., S.P.);Institut National de la Recherche Agronomique, Institute Jean-Pierre Bourgin, 78026 Versailles, France (S.V.);Department of Botany and Plant Sciences, University of California, Riverside, California 92521 (G.H.);Department of Plant and Microbial Biology, North Caroline State University, Raleigh, North Carolina 27695 (J.A.);Australian Research Council Centre of Excellence in Plant Cell Walls, School of Botany, University of Melbourne, Parkville, Victoria 3010, Australia (S.P.); andDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305 (D.E.).
  • 2 Departments of Plant Sciences (N.W., T.E.W., V.E.E., J.L., G.D.) and Veterinary Medicine (R.J., B.W.), University of California, Davis, California 95616;Max-Planck-Institute of Molecular Plant Physiology, Science Campus, 14476 Golm, Germany (R.L., S.P.);Institut National de la Recherche Agronomique, Institute Jean-Pierre Bourgin, 78026 Versailles, France (S.V.);Department of Botany and Plant Sciences, University of California, Riverside, California 92521 (G.H.);Department of Plant and Microbial Biology, North Caroline State University, Raleigh, North Carolina 27695 (J.A.);Australian Research Council Centre of Excellence in Plant Cell Walls, School of Botany, University of Melbourne, Parkville, Victoria 3010, Australia (S.P.); andDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305 (D.E.) gdrakakaki@ucdavis.edu.
Abstract

Cellulose synthase complexes (CSCs) at the plasma membrane (PM) are aligned with cortical microtubules (MTs) and direct the biosynthesis of cellulose. The mechanism of the interaction between CSCs and MTs, and the cellular determinants that control the delivery of CSCs at the PM, are not yet well understood. We identified a unique small molecule, CESA TRAFFICKING INHIBITOR (CESTRIN), which reduces cellulose content and alters the anisotropic growth of Arabidopsis (Arabidopsis thaliana) hypocotyls. We monitored the distribution and mobility of fluorescently labeled cellulose synthases (CESAs) in live Arabidopsis cells under chemical exposure to characterize their subcellular effects. CESTRIN reduces the velocity of PM CSCs and causes their accumulation in the cell cortex. The CSC-associated proteins KORRIGAN1 (KOR1) and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1 (CSI1) were differentially affected by CESTRIN treatment, indicating different forms of association with the PM CSCs. KOR1 accumulated in bodies similar to CESA; however, POM2/CSI1 dissociated into the cytoplasm. In addition, MT stability was altered without direct inhibition of MT polymerization, suggesting a feedback mechanism caused by cellulose interference. The selectivity of CESTRIN was assessed using a variety of subcellular markers for which no morphological effect was observed. The association of CESAs with vesicles decorated by the trans-Golgi network-localized protein SYNTAXIN OF PLANTS61 (SYP61) was increased under CESTRIN treatment, implicating SYP61 compartments in CESA trafficking. The properties of CESTRIN compared with known CESA inhibitors afford unique avenues to study and understand the mechanism under which PM-associated CSCs are maintained and interact with MTs and to dissect their trafficking routes in etiolated hypocotyls.

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