Search bioRxiv⌕ Search

Biology subjects

Teh, O.-k.

Publications and source records attributed to Teh, O.-k..

2 recordsLinked to original sources

Glycosylation-dependent sorting of an Arabinogalactan protein SLEEPING BEAUTY mediates apical tip growth and osmosensing in Physcomitrium patens

Polarized tip growth is a key morphological adaption that facilitated land plant terrestrialization, and arabinogalactan proteins (AGPs) are central regulators of this process. However, how glycosylation modulates AGP function during tip growth remains poorly understood. Here, we show that the AGP SLEEPING BEAUTY (SB) is required for cell wall integrity during protonemal tip growth in the moss Physcomitrium patens, a function that is conserved in the distantly related vascular plant Arabidopsis thaliana. Loss of SB function disrupts cellulose microfibril organization and compromises cell wall integrity, leading to altered tip growth dynamics and geometry. Using a hypoglycosylated SB variant, we demonstrate that glycosylation of Pro55, Pro92, and Pro94 within a highly intrinsically disordered region is required for proper SB secretion and vacuolar trafficking; loss of these modifications results in pronounced inhibition of tip growth. We propose that glycosylation of the intrinsically disordered domain in AGP fine-tunes SB abundance at the cell surface, thereby facilitating cellulose microfibril biosynthesis and/or assembly to regulate robust polarized tip growth.

plant biology↗

Phosphorylation of the exocyst subunit Exo70B2 contributes to the regulation of its function

The exocyst is a conserved hetero-octameric complex that mediates early tethering of post-Golgi vesicles during exocytosis. Its Exo70 subunit functions as a spatiotemporal regulator by mediating numerous interactions with proteins and lipids. However, a molecular understanding of the exocyst functions remains challenging. Exo70B2 localized to dynamic foci at the plasma membrane and transited through Brefeldin A (BFA)-sensitive compartments, indicating that it participates in conventional secretion. Conversely, treatment with the immunogenic peptide flg22 or the salicylic acid (SA) defence hormone analogue Benzothiadiazole (BTH), induced Exo70B2 transport into the vacuole where it colocalized with autophagic markers AUTOPHAGY-RELATED PROTEIN 8 (ATG8) and NEIGHBOR OF BRCA1 GENE 1 (NBR1). According with its role in immunity, we discovered that Exo70B2 interacts with and is phosphorylated by the MITOGEN-ACTIVATED PROTEIN KINASE 3 (MPK3). Mimicking phosphorylation inhibited Exo70B2 localization at sites of active secretion. By contrast, lines expressing phosphonull variants displayed higher Effector-Triggered Immunity and were hypersensitive to BTH, conditions known to induce the secretory pathway. Our results suggest a molecular mechanism by which phosphorylation of Exo70B2 regulates interaction with the plasma membrane, and couples the secretory pathway with cellular signalling.

cell biology↗