Endosidin20 does not affect cellulose synthase complex transport from ER to the Golgi

The deposition of cellulose is a defining aspect of plant growth and development, but regulation of this process is poorly understood. Here, we demonstrate that the protein kinase BRASSINOSTEROID INSENSITIVE2 (BIN2), a key negative regulator of brassinosteroid (BR) signaling, can phosphorylate Arabidopsis cellulose synthase A1 (CESA1), a subunit of the primary cell wall cellulose synthase complex, and thereby negatively regulate cellulose biosynthesis. Accordingly, point mutations of the BIN2-mediated CESA1 phosphorylation site abolished BIN2-dependent regulation of cellulose synthase activity. Hence, we have uncovered a mechanism for how BR signaling can modulate cellulose synthesis in plants.

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The Cellulase KORRIGAN Is Part of the Cellulose Synthase Complex

PLANT PHYSIOLOGY ◽

10.1104/pp.114.241216 ◽

2014 ◽

Vol 165 (4) ◽

pp. 1521-1532 ◽

Cited By ~ 89

Author(s):

Thomas Vain ◽

Elizabeth Faris Crowell ◽

Hélène Timpano ◽

Eric Biot ◽

Thierry Desprez ◽

...

Keyword(s):

Cellulose Synthase ◽

Cellulose Synthase Complex

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Cellulose biosynthesis in higher plants

Acta Societatis Botanicorum Poloniae ◽

10.5586/asbp.1996.003 ◽

2014 ◽

Vol 65 (1-2) ◽

pp. 17-24 ◽

Cited By ~ 1

Author(s):

Krystyna Kudlicka ◽

R. M. Brown, Jr

Keyword(s):

Higher Plants ◽

Regulatory Protein ◽

Cellulose Synthase ◽

Cell Disruption ◽

Cellulose Synthesis ◽

Higher Plant ◽

Cellulose Synthase Complex ◽

Enzyme Complexes

Knowledge of the control and regulation of cellulose synthesis is fundamental to an understanding of plant development since cellulose is the primary structural component of plant cell walls. In vivo, the polymerization step requires a coordinated transport of substrates across membranes and relies on delicate orientations of the membrane-associated synthase complexes. Little is known about the properties of the enzyme complexes, and many questions about the biosynthesis of cell wall components at the cell surface still remain unanswered. Attempts to purify cellulose synthase from higher plants have not been successful because of the liability of enzymes upon isolation and lack of reliable in vitro assays. Membrane preparations from higher plant cells incorporate UDP-glucose into a glucan polymer, but this invariably turns out to be predominantly β -1,3-linked rather than β -1,4-linked glucans. Various hypotheses have been advanced to explain this phenomenon. One idea is that callose and cellulose-synthase systems are the same, but cell disruption activates callose synthesis preferentially. A second concept suggests that a regulatory protein as a part of the cellulose-synthase complex is rapidly degraded upon cell disruption. With new methods of enzyme isolation and analysis of the in vitro product, recent advances have been made in the isolation of an active synthase from the plasma membrane whereby cellulose synthase was separated from callose synthase.

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