{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Ying Miao"],"species":["Arabidopsis Thaliana"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0004387000"],"submitter_email":["ymiao@fafu.edu.cn"],"submitter_affiliation":["Fujian Provincial Key Laboratory of Functional Biology, Fujian Agriculture and Forestry University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["The translocation of proteins between various compartments of cells is the simplest and most direct way of an/retrograde communication. However, the mechanism of protein trafficking is far understood. In this study, we showed that the alteration of WHY2 protein abundance in various compartments of cells was dependent on a HECT-type ubiquitin E3 ligase UPL5 interacting with WHY2 in the cytoplasm, plastid, and nucleus, as well as mitochondrion to selectively ubiquitinate various Kub-sites (Kub 45 and Kub 227) of WHY2. Plastid genome stability can be maintained by the UPL5-WHY2 module, accompany by the alteration of photosystem activity and senescence-associated gene expression. In addition, the specificity of UPL5 ubiquitinating various Kub-sites of WHY2 was responded to cold or CaCl<sub>2</sub> stress, in a dose [Ca<sup>2+</sup>]<sub>cyt</sub>-dependent manner. This demonstrates the integration of the UPL5 ubiquitination with the regulation of WHY2 distribution and retrograde communication between organelle and nuclear events of leaf senescence.","Catabolism of macromolecules is a major event in senescent cells, especially involving proteolysis of organelles and abnormally aggregated proteins, circulation of nutrients, and precise control of intracellular environmental balance. Proteasomes are distributed in the nucleus and cytoplasm; however, proteasomes in organelles are limited. In this study, multi-omics proteomic analyses of ubiquitinated proteins enriched by using antibody against \"di-Gly-Lys\" via a free labeling were used to investigate the global changes of protein levels and ubiquitination modification levels of <i>upl5</i> mutant relative to wild-type plant; subcellular localization analysis of UPL5 was found to be located in the nucleus, cytoplasm, and plastid within the cell; and the direct lysine site patterns of UPL5 were screened by the H89R substitution in the tagged ubiquitinated assay. It suggests that UPL5 acting as a candidate of organelle E3 ligase either in the nucleus or cytoplasm or plastid modifies numerous targets related to nuclear transcription and plastid photosynthesis involving in Ca<sup>2+</sup> and hormone signaling pathway in plant senescence and in response to (a)biotic stress protection."],"pubmed_title":["Establishment of a Landscape of UPL5-Ubiquitinated on Multiple Subcellular Components of Leaf Senescence Cell in <i>Arabidopsis</i>.","UPL5 modulates WHY2 protein distribution in a Kub-site dependent ubiquitination in response to [Ca<sup>2+</sup>]<sub>cyt</sub>-induced leaf senescence."],"pubmed_authors":["Lan Wei W, Zheng Shuai S, Yang Ping P, Qiu Yuhao Y, Xu Yun Y, Miao Ying Y","Lan Wei W, Ma Weibo W, Zheng Shuai S, Yang Ping P, Qiu Yuhao Y, Lin Wenfang W, Ren Yujun Y, Miao Ying Y"],"additional_accession":[]},"is_claimable":false,"name":"Establishment of a landscape of UPL5-ubiquitinated on multiple subcellular components of leaf senescence cell in Arabidopsis","description":"Catabolism of macromolecules is a major event in senescent cells, especially involving proteolysis of organelles and abnormally aggregated proteins, the circulation of nutrients, and precise control of intracellular environmental balance. Proteasomes are distributed in the nucleus and cytoplasm; however, proteasome in organelles is limited. In this study, multi-omics proteomic analyses of ubiquitinated proteins enriched by using antibody against “di-Gly-Lys” via a free labeling was used to investigate the global changes of protein levels and ubiquitination modification levels of upl5 mutant relative to wildtype plant; subcellular localization analysis of UPL5 was found to be located in the nucleus, cytoplasm and plastid within the cell; and the direct lysine site pattern of UPL5 were screened by the H89R substitution in the tagged ubiquitinated assay. It suggests that UPL5 acting as a candidate of organelle E3 ligase either in the nucleus or cytoplasm or plastid, modifies numerous targets related to nuclear transcription and plastid photosynthesis involving in Ca2+ and hormone signaling pathway in plant senescence and in response to (a)biotic stress protection.","dates":{"publication":"Sat Apr 30 00:00:00 BST 2022"},"accession":"PXD033568","cross_references":{"TAXONOMY":["3702"],"pubmed":["35628561","36994183"]}}