<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Heng Yin</submitter><species>Arabidopsis Thaliana</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0002920000</full_dataset_link><submitter_email>yinheng@dicp.ac.cn</submitter_email><submitter_affiliation>Dalian Institute of Chemical Physics, Chinese Academy of Sciences.</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol><pubmed_abstract>As an essential enzyme in the uridine diphosphate (UDP)-GlcNAc biosynthesis pathway, the significant role of N-acetylglucosamine phosphate mutase (AGM) remains unknown in plants. In the present study, a functional plant AGM (AtAGM) was identified from Arabidopsis thaliana. AtAGM catalyzes the isomerization of GlcNAc-1-P and GlcNAc-6-P, and has broad catalytic activity on different phosphohexoses. UDP-GlcNAc contents were significantly decreased in AtAGM T-DNA insertional mutants, which caused temperature-dependent growth defects in seedlings and vigorous growth in adult plants. Further analysis revealed that protein O-GlcNAcylation but not N-glycosylation was dramatically impaired in Atagm mutants due to UDP-GlcNAc shortage. Combined with the results from O-GlcNAcylation or N-glycosylation deficient mutants, and O-GlcNAcase inhibitor all suggested that protein O-GlcNAcylation impairment mainly leads to the phenotypic variations of Atagm plants. In conclusion, based on the essential role in UDP-GlcNAc biosynthesis, AtAGM is important for plant growth mainly via protein O-GlcNAcylation-level regulation.</pubmed_abstract><pubmed_title>Protein O-GlcNAcylation impairment caused by N-acetylglucosamine phosphate mutase deficiency leads to growth variations in Arabidopsis thaliana.</pubmed_title><pubmed_authors>Jia Xiaochen X, Zhang Hongyan H, Qin Hongqiang H, Li Kuikui K, Liu Xiaoyan X, Wang Wenxia W, Ye Mingliang M, Yin Heng H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Impaired O-GlcNAcylation rather than N-glycosylation caused by AtAGM deficiency leads to growth variations in Arabidopsis thaliana</name><description>To reveal the function of N-acetylglucosamine phosphate mutase (AGM) and UDP-GlcNAc in Arabidopsis growth, WT and a T-DNA insertional mutant Atagm-2 were used for proteomic analysis.</description><dates><publication>Thu Mar 25 00:00:00 GMT 2021</publication></dates><accession>PXD024977</accession><cross_references><TAXONOMY>3702</TAXONOMY><pubmed>36799458</pubmed></cross_references></HashMap>