Plant Cell Advance Publication. Published on May 14, 2020, doi:10.1105/tpc.20.

00382

IN BRIEF

Endosidin20: A Key to Unlock the Secrets of Cellulose Biosynthesis

By now, you would think we’d know

everything about cellulose, given its status as
the most abundant biopolymer on Earth and
its simple chemical composition. Cellulose is
composed of β-1,4-D-glucose units
assembled into straight chain polymers.
These rod-like molecules are packed into
strong microfibrils held tightly together by
hydrogen bonds and van der Waals forces.
Cellulose provides plant cell walls with the
mechanical strength needed to resist turgor
pressure while affecting the size, shape, and
direction of cell growth and division, thereby
shaping plant morphology (Saxena and
Brown, 2005). Although both paper and cotton
(Gossypium hirsutum) fibers contain over
90% cellulose, and cellulose is used to make
everything from ice cream to biofuel, we still
don’t understand exactly how plants
synthesize this polymer. We do know that
elegant cellulose synthase (CESA) complexes
(CSCs) are assembled in the endoplasmic
reticulum or Golgi apparatus and delivered to
the plasma membrane (PM), where they
actively synthesize cellulose from uridine
diphosphate (UDP)-glucose in the cytosol
(reviewed in Polko and Kieber, 2019).
However, how CESAs catalyze cellulose
synthesis is unclear, and how this catalytic
activity affects CSC trafficking is unknown.
CSCs are little machines composed of
three isoforms of monomeric CESAs arranged
in six-fold symmetrical rosettes at a 1:1:1
ratio. Each complex contains a cytoplasmic
catalytic domain, transmembrane regions,
plant-conserved sequences, and class-
specific regions thought to facilitate CSC
assembly and trafficking. However, the lack of
tools to probe cellulose biosynthesis, such as
CESA inhibitors with known modes of action,
has hampered efforts to explore CSC activity.
In a Breakthrough Report, Huang et al.
(2020) describe the small molecule
Endosidin20 (ES20), a powerful new cellulose
synthesis inhibitor that directly targets the
Arabidopsis thaliana (Arabidopsis) CESA
isoform CESA6.
A chemical library screen identified
ES20, which markedly alters Arabidopsis
seedling morphology by reducing cellulose
levels. More than a dozen ethyl
ES20 treatment reduces the abundance of plasma membrane-localized YFP-
CESA6 in root epidermal cells. Representative images of plasma membrane-localized
YFP-CESA6 (CESA6 fused with yellow fluorescent protein) in root epidermal cells after
control (0.1% DMSO) or 6 µM ES20 treatment are shown. Scale bars, 5 µM (Reprinted
from Huang et al. [2020], Figure 5E.)
methanesulfonate-induced mutants that grew subcellular trafficking of CSCs. While this
well on ES20 harbored mutations in CESA6, observation is intriguing, the relationship
suggesting that ES20 directly affects CESA6 between CESA catalytic activity and CSC
activity. Topological analysis, structural trafficking is complicated and requires further
modeling, and molecular docking analysis study. Perhaps ES20 could be used in
indicated that ES20 targets the UDP-glucose conjunction with a collection of fluorescently
binding site (i.e., catalytic site) of CESA6 to tagged CESA6 with mutations at the catalytic
inhibit cellulose polymerization; the authors site to explore the effects of CESA catalytic
confirmed this by analyzing mutant forms of activity on CSC trafficking and the underlying
CESA6. The authors performed several molecular mechanisms and shed light on the
biochemical assays to show that ES20 targets mysterious process of cellulose biosynthesis.
CESA6 directly, finding that it competes with
UDP-glucose for direct binding to this CESA. Jennifer Lockhart
To explore whether the catalytic activity Science Editor
of plant CESAs affects intracellular trafficking, jlockhart@aspb.org
the authors examined the effects of ES20 on ORCID: 0000-0002-1394-8947
CSC localization and dynamics in transgenic
seedlings expressing CESA6 fused to yellow REFERENCES
fluorescent protein in the cesa6 loss-of-
function background using high-resolution live Huang, L. et al. (2020). Endosidin20 targets
cell imaging of root epidermal cells. ES20 the cellulose synthase catalytic domain to
treatment significantly reduced the rate of inhibit cellulose biosynthesis. Plant Cell 32:
CSC motility at the PM, confirming that ES20 doi:10.1015/tpc00202.2020.
inhibits CSC catalytic activity. ES20 treatment Polko, J.K. and Kieber, J.J. (2019). The
also decreased the density of PM-localized regulation of cellulose biosynthesis in
CSCs (see figure), reduced the delivery of plants. Plant Cell 31, 282-296.
CSC to the PM, and increased the abundance Saxena, I.M. and Brown, R.M. (2005).
of CSC at the Golgi, indicating that the Cellulose biosynthesis: Current views and
catalytic activity of CESA6 affects the evolving concepts. Ann. Bot. 96: 9-21.

©2020 American Society of Plant Biologists. All Rights Reserved

 Endosidin20: A Key to Unlock the Secrets of Cellulose Biosynthesis
Jennifer A Lockhart
Plant Cell; originally published online May 14, 2020;
DOI 10.1105/tpc.20.00382
This information is current as of May 14, 2020

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