Abstract
Plant cell walls are extracellular matrices that surround plant cells and critically influence basic cellular processes, such as cell division and expansion. Cellulose is a major constituent of plant cell walls, and this paracrystalline polysaccharide is synthesized at the plasma membrane by a large protein complex known as the cellulose synthase complex (CSC). Recent efforts have identified numerous protein components of the CSC, but relatively little is known about regulation of cellulose biosynthesis. Numerous phosphoproteomic surveys have identified phosphorylation events in CSC associated proteins, suggesting that protein phosphorylation may represent an important regulatory control of CSC activity. In this review, we discuss the composition and dynamics of the CSC in vivo, the catalog of CSC phosphorylation sites that have been identified, the function of experimentally examined phosphorylation events, and potential kinases responsible for these phosphorylation events. Additionally, we discuss future directions in cellulose synthase kinase identification and functional analyses of CSC phosphorylation sites.
Highlights
Plant cell walls are complex polysaccharide-rich extracellular matrices that surround all plant cells and critically influence basic plant cellular growth processes, such as cell expansion, cell division, and acquisition of cell shape (Somerville et al, 2004; Cosgrove, 2005)
While the functional implications of these phosphorylation sites remain to be determined in vivo, these findings suggest that phosphorylation of CESA7 may regulate the stability of the secondary cellulose synthase complex (CSC), and these results agree with investigations of the secondary CSC in living cells (Taylor, 2007)
This is a complex and combinatorial problem because most plant genomes contain over 1000 protein kinases, and numerous experimentally supported phosphorylation sites exist in the CSC
Summary
Cellulose is a major constituent of plant cell walls, and this paracrystalline polysaccharide is synthesized at the plasma membrane by a large protein complex known as the cellulose synthase complex (CSC). Recent efforts have identified numerous protein components of the CSC, but relatively little is known about regulation of cellulose biosynthesis. Numerous phosphoproteomic surveys have identified phosphorylation events in CSC associated proteins, suggesting that protein phosphorylation may represent an important regulatory control of CSC activity. We discuss the composition and dynamics of the CSC in vivo, the catalog of CSC phosphorylation sites that have been identified, the function of experimentally examined phosphorylation events, and potential kinases responsible for these phosphorylation events. We discuss future directions in cellulose synthase kinase identification and functional analyses of CSC phosphorylation sites
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