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The Regulation of Cellulose Biosynthesis in Plants

Joanna K. Polko, Joseph J. Kieber
Joanna K. Polko
Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599
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Joseph J. Kieber
Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599
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  • For correspondence: jkieber@unc.edu

Published February 2019. DOI: https://doi.org/10.1105/tpc.18.00760

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    Figure 1.

    Schematic Representations of the Structure of a CESA Protein and a CSC.

    (A) Domain structure of a CESA. The intracellular N-terminal domain contains a Zn binding domain and a variable region and is followed by two transmembrane domains. The large cytoplasmic central catalytic domain is divided into the conserved region, which flanks the plant-specific region on both sides, the variable region(s), which includes the class-specific region, and the conserved region(s). The six subsequent transmembrane domains are followed by the cytoplasmic C-terminal domain. CESA1 phosphorylations on various Ser and Thr residues are indicated (source: PhosPhAt 4.0, Zulawski et al., 2013; and references in the text). Several cysteines in the cytoplasmic loop and within the C-terminal domain that are s-acylated in CESA7 (Kumar 2016b) are depicted in pink. C, cellulose chain; CR1, conserved region 1; CR2, conserved region 2; P-CR, plant-specifc region; S, Ser; T, Thr.

    (B) A schematic representation of a CSC consisting of 18 individual CESA proteins. The model is consistent with the rules outlined by Hill et al. (2014) and assumes that: a CSC is composed of six lobes that contain three CESA isoforms; the contacts between different isoforms is conserved; and the number of CESAs in each lobe is divisible by three.

    (C) A model of a cellulose microfibril consisting of five layers of cellulose chains in a “34443” arrangement (C = cellulose chain).

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    Figure 2.

    A Cartoon of CSC Trafficking and the Other Components of the CSC Machinery.

    CSCs are assembled in the Golgi apparatus where they physically interact with STL proteins that assist their assembly and distribution in the Golgi. CSCs move through the TGN and follow the exocytosis route to the PM, where their insertion sites coincide with the pausing of the Golgi along the CMTs. The insertion of CSCs in the PM is preceded by POM2/CSI1, the exocyst complex, and PTL, which are required for CSC delivery. The CESA-interacting proteins SHOU4/4L negatively affect CSC exocytosis. POM2/CSI1 proteins also act as linkers between CSCs and CMTs and are necessary for the formation of SmaCCs/MASCs. The CC1 and CC2 belong to the CSCs, associate with SmaCCs/MASCs under salt stress and mediate the CMT and CSC dynamics, allowing for their recovery. CMU proteins regulate proper CMT spacing during cellulose biosynthesis. KOR is a component of CSCs required for optimal cellulose biosynthesis and COB is necessary for proper microfibril orientation. The SOS5 and FEI1/2 leucine-rich repeat-RLKs mediate cellulose biosynthesis and CrRLK1L THE1 inhibits cell expansion upon perturbation of cellulose biosynthesis. CSCs undergo CME that requires the AP2 complex and TPLATE complex members such as TWD40-1, TPLATE, and TML. The endocytosed CSCs may undergo recycling back to the PM or might be targeted for degradation.

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    Table 1. CESA Interacting Proteins
    ProteinPutative rolePartner CESAMethodaReference
    KORRIGANCellulose synthesis and CSC traffickingCESA1Gel filtration,(Vain et al., 2014)
    CESA3Split-ubiquitin for membrane proteins,(Zhu et al., 2018)
    CESA6BiFC,(Mansoori et al., 2014)
    CESA4GFP-TRAP/MS,
    CESA8Y2H
    CC1/2Cellulose synthesis during salt stressCESA1Split-ubiquitin assay in yeast(Endler et al., 2015)
    CESA3
    CESA6
    POM2/CSI1CSC-CMT interaction; formation of SmaCCs/MASCs; CSC traffickingCESA1CESA3Y2H, GST pull-down(Gu et al., 2010)(Lei et al., 2015)
    CESA6
    AP2M/µ2CSC endocytosisCESA1Split-ubiquitin Y2H,(Bashline et al., 2013)
    CESA3GST pull-down
    CESA6
    Sec5BCSC exocytosisCESA6Y2H,(Zhu et al., 2018)
    Sec10GFP-TRAP/MS
    Sec6
    Sec15B
    Sec8
    Sec3A
    Exo84B
    Exo70B1
    Exo70A1
    PTL1
    TMLCSC endocytosisCESA6Co-IP, BiFC(Sanchez-Rodriguez et al., 2018)
    TPLATE
    BIN2CESA phosphorylation; regulation of CESA activityCESA1in vitro protein kinase assay(Sanchez-Rodriguez et al., 2017)
    SHOU4CSC exocytosisCESA1Y2H, Co-IP(Polko et al., 2018)
    CESA3
    CESA6
    • ↵a The methods shown are not necessarily for all the partner CESAs indicated. BIFC, bimolecular fluorescence complementation; Co-IP, co-immunoprecipitation; GST, glutathione S-transferase; Y2H, yeast two-hybrid.

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The Regulation of Cellulose Biosynthesis in Plants
Joanna K. Polko, Joseph J. Kieber
The Plant Cell Feb 2019, 31 (2) 282-296; DOI: 10.1105/tpc.18.00760

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The Regulation of Cellulose Biosynthesis in Plants
Joanna K. Polko, Joseph J. Kieber
The Plant Cell Feb 2019, 31 (2) 282-296; DOI: 10.1105/tpc.18.00760
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  • Article
    • Abstract
    • INTRODUCTION
    • STRUCTURE OF CSCs
    • POSTTRANSLATIONAL REGULATION OF CSCs
    • CESA ASSEMBLY AND CELLULAR TRAFFICKING
    • ADDITIONAL CSC-INTERACTING COMPONENTS
    • CELLULOSE AND PLANT CELL WALL INTEGRITY MAINTENANCE
    • CONCLUSIONS AND OUTSTANDING QUESTIONS
    • Dive Curated Terms
    • Acknowledgments
    • AUTHOR CONTRIBUTIONS
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The Plant Cell: 31 (2)
The Plant Cell
Vol. 31, Issue 2
Feb 2019
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