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Protein O-glycosylation regulates diverse developmental and defense processes in plants

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Summary: The recent discovery of SPY-catalyzed protein O-fucosylation provides new insights into the regulation of nucleocytoplasmic protein functions in plants. This study identified hundreds of O-fucosylated proteins and demonstrated the involvement of SPY in sugar-dependent growth in Arabidopsis. The findings shed light on the signaling network underlying sugar regulation of plant growth and development.

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O-glycosylation of the extracellular domain of pollen class I formins modulates their plasma membrane mobility

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Summary: In Arabidopsis pollen tubes, class I formins play a crucial role in organizing actin arrays during tube elongation, with their localization and mobility being dependent on O-glycosylation of their extracellular domain. The extracellular domain is necessary for the function of two pollen-expressed class I formins, AtFH3 and AtFH5, and specific O-glycans are attached to these sequences. Loss of O-glycosylation alters membrane localization and disrupts actin organization. The different O-glycans also affect lateral mobility in the plasma membrane. This study highlights the importance of protein sub-functionalization in pollen tube elongation.

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Summary: This review highlights recent advances in the analysis of protein O-glycosylation, including the release of O-glycans, site-specific elucidation of intact O-glycopeptides, identification of O-glycosites, characterization of different O-glycoproteases, mass spectrometry fragmentation methods for site-specific O-glycosylation assignment, and O-glycosylation data analysis. Additionally, the role of O-glycosylation in health and disease is discussed.

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O-fucosylation of CPN20 by SPINDLY Derepresses Abscisic Acid Signaling During Seed Germination and Seedling Development

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