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Lampugnani, E. R.

Publications and source records attributed to Lampugnani, E. R..

2 recordsLinked to original sources

Tip Growth Defective1 interacts with the cellulose synthase complex to regulate cellulose synthesis in Arabidopsis thaliana.

Plant cells possess robust and flexible cell walls composed primarily of cellulose, a polysaccharide that provides structural support and enables cell expansion. Cellulose is synthesised by the Cellulose Synthase A (CESA) catalytic subunits, which form cellulose synthase complexes (CSCs). While significant progress has been made in unravelling CSC function, the trafficking of CSCs and the involvement of post-translational modifications in cellulose synthesis remain poorly understood. In order to deepen our understanding of cellulose biosynthesis, this study utilised immunoprecipitation techniques with CESA6 as the bait protein to explore the CSC and its interactors. We successfully identified the core proteins of the CSC complex and discovered new potential interactors involved in CSC trafficking and the coordination of cell wall synthesis. Moreover, we identified TIP GROWTH DEFECTIVE 1 (TIP1) protein S-acyl transferases (PATs) as an interactor of the CSC complex. We confirmed the interaction between TIP1 and the CSC complex through multiple independent approaches. Further analysis revealed that tip1 mutants exhibited stunted growth and reduced levels of crystalline cellulose in leaves. These findings suggest that TIP1 positively influences cellulose biosynthesis, potentially mediated by its role in the S-acylation of the CSC complex.

plant biology↗

Control of PHYTOCHROME KINASE SUBSTRATE subcellular localization and biological activity by protein S-acylation

PHYTOCHROME KINASE SUBSTRATE (PKS) proteins are involved in light-regulated growth orientation responses. They act downstream of phytochromes to control hypocotyl gravitropism in the light and act early in phototropin signaling. Despite their importance for plant development, little is known about their molecular mode of action except that they belong to a protein complex comprising the phototropins at the plasma membrane. Identifying evolutionarily conservation is one approach to reveal biologically important protein motifs. Here, we show that PKS sequences are restricted to seed plants and that these proteins share 6 motifs (A to F from the N- to the C-terminus). While motif D is also found in BIG GRAIN proteins the remining domains are PKS specific. We provide evidence that motif C is S-acylated on highly conserved cysteines, which mediates PKS protein association with the plasma membrane. This motif is also required for PKS4-mediated phototropism and control of hypocotyl gravitropism in the light. Finally, our data suggests that the mode of PKS4 plasma membrane association is important for its biological activity. Our work identifies the mode of plasma membrane association of PKS proteins and strongly suggests that this is their site of action to modulate environmentally regulated organ positioning.

plant biology↗