SPINDLY and SECRET AGENT-mediated Protein Glycosylation Regulates Plant Development and Stress Response

doi:10.13560/j.cnki.biotech.bull.1985.2024-0916

Abstract

Abstract:

Protein glycosylation modifications play a crucial role in regulating numerous biological processes, with significant advancements made, particularly in the areas of plant and animal development as well as responses to abiotic and biotic stressors. O-GlcNAcylation (O-GlcNAc) and O-Fucosylation (O-Fuc) are two important types of protein modifications. Among them, SECRET AGENT (SEC) and SPINDLY (SPY) are key homologous proteins of O-GlcNAc transferase (OGT), responsible for O-GlcNAc modification and O-Fuc modification, respectively. They play crucial roles in plant growth, development, and stress response processes. This review provides a comprehensive overview of the O-GlcNAc and O-Fuc modification processes of proteins and their associated enzymes. It analyses the evolutionary characteristics of SEC and SPY, highlights their regulatory mechanisms in plant development and stress responses, and discusses future research hotspots and challenges in plant protein glycosylation modifications.

Key words: O-GlcNAcylation, O-Fucosylation, plant development, response to adversity

FAN Yue-ni, XIAN Bao-shan, SHI Yi-ping, REN Meng-yuan, XU Jia-hui, WEI Shao-wei, XU Xiao-jing, LUO Xiao-feng, SHU Kai. SPINDLY and SECRET AGENT-mediated Protein Glycosylation Regulates Plant Development and Stress Response[J]. Biotechnology Bulletin, 2025, 41(4): 1-8.

Figures/Tables 2

Fig. 1 Schematic illustration of SPY-mediated O-Fucosylation and SEC-mediated O-GlcNAcylation in plantsA: O-Fuc modification is catalyzed by protein O-fucosyltransferase (POFUT) to link the fucose of GDP-Fucose to the hydroxyl oxygen of the serine (Ser) or threonine (Thr) residue side chain of the protein. B: O-GlcNAc modification is catalyzed by O-GlcNAc transferase (OGT) to link GlcNAc in UDP-GlcNAc to serine (Ser) or threonine (Thr) residue side-chain hydroxyl oxygen of proteins. In animals, O-GlcNAcases (OGA) can remove GlcNAc, and only OGA analogues are currently found in plants

Fig. 2 Schematic representation of the protein domains of SPY and SEC in Arabidopsis thalianaA: Protein domains of SPY and SEC in Arabidopsis thaliana were predicted using the SMART: Main page. Both SPY and SEC include the TPR domain and catalytic domain. Gray boxes indicate low complexity. B: SWISS-MODEL was used to predict the protein domain ofSPY in in A. thaliana, and the local amplification region was the binding site of GDP-Fucose. SPY can form a head-to-tail dimer conformation and fucosylate itself. C: SWISS MODEL was utilized to predict the protein domain of SEC in in A. thaliana

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