The regulation of the cell wall by glycosylphosphatidylinositol-anchored proteins in Arabidopsis

Abstract

A polysaccharides-based cell wall covers the plant cell, shaping it and protecting it from the harsh environment. Cellulose microfibrils constitute the cell wall backbone and are embedded in a matrix of pectic and hemicellulosic polysaccharides and glycoproteins. Various environmental and developmental cues can regulate the plant cell wall, and diverse glycosylphosphatidylinositol (GPI)-anchored proteins participate in these regulations. GPI is a common lipid modification on eukaryotic proteins, which covalently tethers the proteins to the membrane lipid bilayer. Catalyzed by a series of enzymic complexes, protein precursors are post-translationally modified at their hydrophobic carboxyl-terminus in the endomembrane system and anchored to the lipid bilayer through an oligosaccharidic GPI modification. Ultimately, mature proteins reach the plasma membrane via the secretory pathway facing toward the apoplast and cell wall in plants. In Arabidopsis, more than three hundred GPI-anchored proteins (GPI-APs) have been predicted, and many are reported to be involved in diverse regulations of the cell wall. In this review, we summarize GPI-APs involved in cell wall regulation. GPI-APs are proposed to act as structural components of the cell wall, organize cellulose microfibrils at the cell surface, and during cell wall integrity signaling transduction. Besides regulating protein trafficking, the GPI modification is potentially governed by a GPI shedding system that cleaves and releases the GPI-anchored proteins from the plasma membrane into the cell wall.

The modified activity of prolyl 4 hydroxylases (P4Hs) reveals the effect of arabinogalactan proteins (AGPs) on changes in the cell wall during the tomato ripening process

“…Our previous studies have shown that there are substantial changes in the structure and distribution of arabinogalactan proteins (AGPs) correlated with the ongoing ripening process (Kutyrieva-Nowak et al, 2023a). As common components in the plant extracellular matrix, AGPs are attached to the plasma membrane via glycosylphosphatidylinositol (GPI) anchors in the C-terminal domain (Showalter, 2001; Lopez-Hernandez et al, 2020; Zhou, 2022; Leszczuk et al, 2023). The specific and mutable distribution of AGPs in the cell wall-plasma membrane continuum allows identification of the effects of these molecules on the specific arrangement of the cell wall assembly in fruit cells (Liu et al, 2015; Leszczuk et al, 2018).…”

The modified activity of prolyl 4 hydroxylases reveals the effect of arabinogalactan proteins on changes in the cell wall during the tomato ripening process

“…Our previous studies have shown that there are substantial changes in the structure and distribution of arabinogalactan proteins (AGPs) correlated with the ongoing ripening process ( Kalaitzis et al., 2023 ; Kutyrieva-Nowak et al., 2023a ). As common components in the plant extracellular matrix, AGPs are attached to the plasma membrane via glycosylphosphatidylinositol (GPI) anchors ( Showalter, 2001 ; Lopez-Hernandez et al., 2020 ; Zhou, 2022 ; Leszczuk et al., 2023 ). The specific and mutable distribution of AGPs in the cell wall-plasma membrane continuum allows identification of the effects of these molecules on the specific arrangement of the cell wall assembly in fruit cells ( Liu et al., 2015 ; Leszczuk et al., 2018 ).…”

CWLP and PRP940 form plasma-membrane nanodomain complexes with aquaporins, interact with PP2A and contribute to dehydration tolerance

“…Flotillins also play a key role in ER to PM-ND trafficking and endocytosis of nonspecific Lipid Transfer Proteins (nsLTPs) that are linked to the PM by glycosylphosphatidylinositol (GPI)anchors (47)(48)(49).…”

“…LatB seems to have a weaker effect on dynamin-dependent endocytosis of FLOT2 (FLOTILLIN 2; another nanodomain marker and binding partner of FLOT1 and aquaporins in Arabidopsis), and its mammalian homologs, which interact with cortical F-actin, dynamins and a range of regulatory proteins (25, 41–46). Flotillins also play a key role in ER to PM-ND trafficking and endocytosis of nonspecific Lipid Transfer Proteins (nsLTPs) that are linked to the PM by glycosylphosphatidylinositol (GPI)-anchors (47–49).…”