{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["https://storage.jpostdb.org/JPST003747/files/20221219_Yoshikawa_B_Fujita_mnTb_protein.xlsx"],"Raw":["https://storage.jpostdb.org/JPST003747/files/225_Yoshikawa_1_mnTb_Tama_FusionIT.raw","https://storage.jpostdb.org/JPST003747/files/227_Yoshikawa_2_mnTb_LUBEL_Tama_FusionIT.raw"],"Other":["https://storage.jpostdb.org/JPST003747/files/20221219_Yoshikawa_B_Fujita_mnTb_1.pdResult"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Fujita Naonobu"],"species":["Drosophila Melanogaster (fruit Fly)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST003747"],"submitter_affiliation":["Institute for Advanced Biosciences, Keio University"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["Transverse tubules (T-tubules) are invaginations of the muscle plasma membrane that facilitate rapid transmission of action potentials, ensuring synchronized muscle contraction. Despite their essential role in muscle physiology, the mechanisms underlying T-tubule formation remain elusive. Here, we identify LUBEL/RNF31, a ubiquitin E3 ligase responsible for linear (M1-linked) ubiquitination, as a key regulator of T-tubule biogenesis in <i>Drosophila</i>. Loss of LUBEL leads to Amphiphysin (Amph)-positive membrane sheets instead of tubular networks. The ubiquitin ligase activity of LUBEL and direct interaction with Amph, a BAR domain protein involved in membrane tubulation, are crucial for proper T-tubule morphology. LUBEL and M1-linked ubiquitin chains assemble into puncta on membranes through multivalent interactions, facilitating Amph-mediated tubulation. Notably, the Amph-LUBEL/RNF31 interaction is evolutionarily conserved across species, underscoring a fundamental role for linear ubiquitination in membrane remodeling. Our findings uncover an unexpected function of linear ubiquitination in membrane deformation driven by BAR proteins."],"pubmed_title":["Linear ubiquitination triggers Amph-mediated T-tubule biogenesis."],"pubmed_authors":["Kawaguchi Kohei K, Hama Yutaro Y, Yoshikawa Harunori H, Nishino Kohei K, Morimoto Kazuki K, Nakamura Tsuyoshi T, Koizumi Michiko M, Sakamaki Yuriko Y, Abe Kota K, Kakuta Soichiro S, Ichimura Koichiro K, Ikeda Fumiyo F, Kosako Hidetaka H, Fujita Naonobu N"],"additional_accession":[]},"is_claimable":false,"name":" Proximity proteomics of T-tubules using miniTurbo-fused LUBEL ","description":"To identify candidate genes unbiasedly, we employed biotinylation-based proximity proteomics of T-tubules in vivo. We generated a transgenic line carrying an LUBEL construct fused with miniTurbo (mnTb). We expressed either LUBEL-mnTb or mnTb alone in muscles, and larvae were reared in the presence or absence of biotin. As a control, LacZ was expressed instead of the mnTb fused constructs. Biotinylated peptides were extracted purified from trypsin-digested samples using Tamavidin 2-REV beads and analyzed by mass spectrometry.","dates":{"publication":"Sat Nov 22 00:00:00 GMT 2025"},"accession":"PXD062634","cross_references":{"TAXONOMY":["7227"],"pubmed":["41499502"]}}