{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Yangnan Gu"],"species":["Arabidopsis Thaliana"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0005894000"],"submitter_email":["guyangnan@berkeley.edu"],"submitter_affiliation":["Department of Plant & Microbial Biology, University of California, Berkeley"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["The nucleocytoplasmic exchange is of fundamental importance to eukaryotic life and is mediated by karyopherins, a superfamily of nuclear transport receptors. However, the function and cargo spectrum of plant karyopherins are largely obscure. Here, we report proximity-labeling-based proteomic profiling of in vivo substrates of KA120, a karyopherin-β required for suppressing autoimmune induction in Arabidopsis. We identify multiple components of the MOS4-associated complex (MAC), a conserved splicing regulatory protein complex. Surprisingly, we find that KA120 does not affect the nucleocytoplasmic distribution of MAC proteins but rather prevents their protein condensation in the nucleus. Furthermore, we demonstrate that MAC condensation is robustly induced by pathogen infection, which is sufficient to activate defense gene expression, possibly by sequestrating negative immune regulators via phase transition. Our study reveals a noncanonical chaperoning activity of a plant karyopherin, which modulates the nuclear condensation of an evolutionarily conserved splicing regulatory complex to coordinate plant immune activation."],"pubmed_title":["Nuclear transport receptor KA120 regulates molecular condensation of MAC3 to coordinate plant immune activation."],"pubmed_authors":["Jia Min M, Chen Xuanyi X, Shi Xuetao X, Fang Yiling Y, Gu Yangnan Y"],"additional_accession":[]},"is_claimable":false,"name":"KA120 negatively regulate immunity through inhibit MOS 4-associated-complex forming nuclear condensates","description":"To understand how KA120 participates in plant immune regulation as a karyopherin-β, we sought to determine in vivo substrates of KA120. We leveraged an enzyme-catalyzed proximity-labeling strategy, in which we fused KA120 with TurboID.  MAC3B could form nuclear condensates in ka120 mutant thus cause aberrant immune response. To investigate how the MAC function may be altered upon condensation and how that may contribute to immune activation, we profiled the composition of the MAC in the presence and absence of KA120.","dates":{"publication":"Thu Feb 23 00:00:00 GMT 2023"},"accession":"PXD040403","cross_references":{"TAXONOMY":["3702"],"pubmed":["37714161"]}}