TY - JOUR AU - Feole, Monica AU - Pozo Devoto, Victorio M. AU - Dragišić, Neda AU - Arnaiz, Cayetana AU - Bianchelli, Julieta AU - Texlová, Kateřina AU - Kovačovicova, Kristina AU - Novotny, Jan S. AU - Havas, Daniel AU - Falzone, Tomas L. AU - Stokin, Gorazd B. TI - Swedish Alzheimer’s disease variant perturbs activity of retrograde molecular motors and causes widespread derangement of axonal transport pathways JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - in press PY - 2024 SP - 107137 SN - 0021-9258 DO - 10.1016/j.jbc.2024.107137 UR - https://m2.mtmt.hu/api/publication/34729098 ID - 34729098 LA - English DB - MTMT ER - TY - JOUR AU - Meng, Wei-Ying AU - Wang, Zi-Xin AU - Zhang, Yunfang AU - Hou, Yujun AU - Xue, Jian-Huang TI - Epigenetic marks or not? The discovery of novel DNA modifications in eukaryotes JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM PY - 2024 SN - 0021-9258 DO - 10.1016/j.jbc.2024.106791 UR - https://m2.mtmt.hu/api/publication/34687917 ID - 34687917 LA - English DB - MTMT ER - TY - JOUR AU - Lavatelli, F. AU - Natalello, A. AU - Marchese, L. AU - Ami, D. AU - Corazza, A. AU - Raimondi, S. AU - Mimmi, M.C. AU - Malinverni, S. AU - Mangione, P.P. AU - Palmer, M.T. AU - Lampis, A. AU - Concardi, M. AU - Verona, G. AU - Canetti, D. AU - Arbustini, E. AU - Bellotti, V. AU - Giorgetti, S. TI - Truncation of the constant domain drives amyloid formation by immunoglobulin light chains JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 4 SN - 0021-9258 DO - 10.1016/j.jbc.2024.107174 UR - https://m2.mtmt.hu/api/publication/34797960 ID - 34797960 N1 - Department of Molecular Medicine, Institute of Biochemistry, University of Pavia, Pavia, Italy Research Area, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy Pathology Unit, Fondazione IRCSS Policlinico San Matteo, Pavia, Italy Department of Medicine (DAME), University of Udine, Udine, Italy Istituto Nazionale Biostrutture e Biosistemi, Roma, Italy Transplant Research Area and Centre for Inherited Cardiovascular Diseases, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy Centre for Amyloidosis, Division of Medicine, University College London, London, United Kingdom Export Date: 18 April 2024 CODEN: JBCHA Correspondence Address: Lavatelli, F.; Department of Molecular Medicine, Italy; email: francesca.lavatelli@unipv.it LA - English DB - MTMT ER - TY - JOUR AU - Szekér, P. AU - Bodó, T. AU - Klima, K. AU - Csóti, Á. AU - Hanh, N.N. AU - Murányi, J. AU - Hajdara, A. AU - Szántó, T.G. AU - Panyi, G. AU - Megyeri, M. AU - Péterfi, Z. AU - Farkas, S. AU - Gyöngyösi, Norbert AU - Hornyák, P. TI - KcsA-Kv1.x chimeras with complete ligand-binding sites provide improved predictivity for screening selective Kv1.x blockers JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 4 PG - 17 SN - 0021-9258 DO - 10.1016/j.jbc.2024.107155 UR - https://m2.mtmt.hu/api/publication/34795149 ID - 34795149 LA - English DB - MTMT ER - TY - JOUR AU - Sonnentag, S.J. AU - Dopler, A. AU - Kleiner, K. AU - Garg, B.K. AU - Mannes, M. AU - Späth, N. AU - Akilah, A. AU - Höchsmann, B. AU - Schrezenmeier, H. AU - Anliker, M. AU - Boyanapalli, R. AU - Huber-Lang, M. AU - Schmidt, C.Q. TI - Triple-fusion protein (TriFu): A potent, targeted, enzyme-like inhibitor of all three complement activation pathways JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 4 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105784 UR - https://m2.mtmt.hu/api/publication/34784555 ID - 34784555 N1 - Institute of Experimental and Clinical Pharmacology, Toxicology and Pharmacology of Natural Products, University of Ulm Medical Centre, Ulm, Germany Eurofins Lancaster Laboratories PSS, Cambridge, United States Institute of Clinical and Experimental Trauma Immunology, University Hospital of Ulm, Ulm, Germany Institute of Transfusion Medicine, University of Ulm, Ulm, Germany Institute of Clinical Transfusion Medicine and Immunogenetics Ulm, German Red Cross Blood Transfusion Service, Baden-Württemberg-Hessen and University Hospital of Ulm, Ulm, Germany Takeda Pharmaceuticals, Cambridge, MA, United States Institute of Pharmacy, Biochemical Pharmacy Group, Martin Luther University Halle-Wittenberg, Halle, Germany Export Date: 11 April 2024 CODEN: JBCHA Correspondence Address: Schmidt, C.Q.; Institute of Experimental and Clinical Pharmacology, Germany; email: christoph.schmidt@uni-ulm.de Chemicals/CAS: alternative complement pathway C3 C5 convertase, 80295-62-1, 80295-67-6; classical complement pathway C3 C5 convertase, 56626-15-4 Tradenames: FACSVerse, Becton Dickinson Manufacturers: Becton Dickinson AB - The introduction of a therapeutic anti-C5 antibody into clinical practice in 2007 inspired a surge into the development of complement-targeted therapies. This has led to the recent approval of a C3 inhibitory peptide, an antibody directed against C1s and a full pipeline of several complement inhibitors in preclinical and clinical development. However, no inhibitor is available that efficiently inhibits all three complement initiation pathways and targets host cell surface markers as well as complement opsonins. To overcome this, we engineered a novel fusion protein combining selected domains of the three natural complement regulatory proteins decay accelerating factor, factor H and complement receptor 1. Such a triple fusion complement inhibitor (TriFu) was recombinantly expressed and purified alongside multiple variants and its building blocks. We analyzed these proteins for ligand binding affinity and decay acceleration activity by surface plasmon resonance. Additionally, we tested complement inhibition in several in vitro/ex vivo assays using standard classical and alternative pathway restricted hemolysis assays next to hemolysis assays with paroxysmal nocturnal hemoglobinuria erythrocytes. A novel in vitro model of the alternative pathway disease C3 glomerulopathy was established to evaluate the potential of the inhibitors to stop C3 deposition on endothelial cells. Next to the novel engineered triple fusion variants which inactivate complement convertases in an enzyme-like fashion, stoichiometric complement inhibitors targeting C3, C5, factor B, and factor D were tested as comparators. The triple fusion approach yielded a potent complement inhibitor that efficiently inhibits all three complement initiation pathways while targeting to surface markers. © 2024 The Authors LA - English DB - MTMT ER - TY - JOUR AU - Zhang, J. AU - Wang, Y. TI - Emerging roles of O-GlcNAcylation in protein trafficking and secretion JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 3 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105677 UR - https://m2.mtmt.hu/api/publication/34760264 ID - 34760264 N1 - Export Date: 27 March 2024 CODEN: JBCHA Correspondence Address: Wang, Y.; Department of Molecular, United States; email: yzwang@umich.edu LA - English DB - MTMT ER - TY - JOUR AU - Moriwaki, T. AU - Terawaki, S. AU - Otomo, T. TI - Impaired lysosomal acidity maintenance in acid lipase-deficient cells leads to defective autophagy JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 3 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105743 UR - https://m2.mtmt.hu/api/publication/34734004 ID - 34734004 N1 - Export Date: 12 March 2024 CODEN: JBCHA Correspondence Address: Otomo, T.; Department of Molecular and Genetic Medicine, Okayama, Japan; email: otomo@med.kawasaki-m.ac.jp LA - English DB - MTMT ER - TY - JOUR AU - Liu, T.-W. AU - Zhao, Y.-M. AU - Jin, K.-Y. AU - Wang, J.-X. AU - Zhao, X.-F. TI - KAT8 is upregulated and recruited to the promoter of Atg8 by FOXO to induce H4 acetylation for autophagy under 20-hydroxyecdysone regulation JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 3 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105704 UR - https://m2.mtmt.hu/api/publication/34733282 ID - 34733282 N1 - Export Date: 12 March 2024 CODEN: JBCHA Correspondence Address: Wang, J.-X.; Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, China; email: jxwang@sdu.edu.cn LA - English DB - MTMT ER - TY - JOUR AU - Jacobs, Ruth Q. AU - Schneider, David A. TI - Transcription elongation mechanisms of RNA polymerases I, II, and III and their therapeutic implications JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 3 PG - 12 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105737 UR - https://m2.mtmt.hu/api/publication/34572620 ID - 34572620 AB - Transcription is a tightly regulated, complex, and essential cellular process in all living organisms. Transcription is comprised of three steps, transcription initiation, elongation, and termination. The distinct transcription initiation and termination mechanisms of eukaryotic RNA polymerases I, II, and III (Pols I, II, and III) have long been appreciated. Recent methodological advances have empowered high-resolution investigations of the Pols’ transcription elongation mechanisms. Here, we review the kinetic similarities and differences in the individual steps of Pol I-, II-, and III-catalyzed transcription elongation, including NTP binding, bond formation, pyrophosphate release, and translocation. This review serves as an important summation of Saccharomyces cerevisiae (yeast) Pol I, II, and III kinetic investigations which reveal that transcription elongation by the Pols is governed by distinct mechanisms. Further, these studies illustrate how basic, biochemical investigations of the Pols can empower the development of chemotherapeutic compounds. LA - English DB - MTMT ER - TY - JOUR AU - Yang, T. AU - Xiao, H. AU - Chen, X. AU - Zheng, L. AU - Guo, H. AU - Wang, J. AU - Jiang, X. AU - Zhang, C.-Y. AU - Yang, F. AU - Ji, X. TI - Characterization of N-glycosylation and its functional role in SIDT1-Mediated RNA uptake JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 300 PY - 2024 IS - 2 SN - 0021-9258 DO - 10.1016/j.jbc.2024.105654 UR - https://m2.mtmt.hu/api/publication/34723554 ID - 34723554 N1 - The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Jiangsu, Nanjing, China Key Laboratory of Protein and Peptide Pharmaceuticals & Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China University of Chinese Academy of Sciences, Beijing, China Chemistry and Biomedicine Innovation Center (ChemBIC), Nanjing University, Jiangsu, Nanjing, China Institute of Artificial Intelligence Biomedicine, Nanjing University, Jiangsu, Nanjing, China Engineering Research Center of Protein and Peptide Medicine, Ministry of Education, Jiangsu, Nanjing, China Export Date: 6 March 2024 CODEN: JBCHA Correspondence Address: Zhang, C.-Y.; The State Key Laboratory of Pharmaceutical Biotechnology, Jiangsu, China; email: cyzhang@nju.edu.cn Chemicals/CAS: RNA, 63231-63-0; Membrane Proteins; Nucleotide Transport Proteins; RNA; SIDT2 protein, human Funding details: National Natural Science Foundation of China, NSFC, 32270139 Funding details: National Key Research and Development Program of China, NKRDPC, 2018YFA0507103 Funding text 1: We thank Qipeng Zhang and Jiatong Tang for valuable assistance and discussion of RNA uptake assay, and Shoubing Zhan for helpful assistance of RT-PCR. We also thank Tongyang Zhu and the National Key Laboratory of Pharmaceutical Biotechnology at Nanjing University in the technical assistance. We are grateful to Jifeng Wang from the Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences for his help with mass spectrometric data acquisition. This work was supported by funds as following dataset. Funding text 2: We thank Qipeng Zhang and Jiatong Tang for valuable assistance and discussion of RNA uptake assay, and Shoubing Zhan for helpful assistance of RT-PCR. We also thank Tongyang Zhu and the National Key Laboratory of Pharmaceutical Biotechnology at Nanjing University in the technical assistance. We are grateful to Jifeng Wang from the Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences for his help with mass spectrometric data acquisition. This work was supported by funds as following dataset. T. Y. H. X. X. C. J. W. and X. J. methodology; T. Y. H. X. and X. C. software; T. Y. H. X. and X. C. validation; T. Y. H. X. and X. C. data curation; T. Y. H. X. and X. C. visualization; T. Y. L. Z. H. G. and X. J. writing–original draft; L. Z. H. G. F. Y. and X. J. investigation; L. Z. F. Y. and X. J. resources; H. G. and X. J. resources; C.-Y. Z. and X. J. supervision; C.-Y. Z. and X. J. project administration; C.-Y. Z. and X. J. funding acquisition; F. Y. and X. J. formal analysis; F. Y. and X. J. writing–review and editing; X. J. formal analysis; X. J. conceptualization. This work was supportedby the National Key Research and Development Program of China 2018YFA0507103 (to X. J.) and also by the National Natural Science Foundation of China 32270139 (to X. J.). AB - The mammalian SID-1 transmembrane family members, SIDT1 and SIDT2, are multipass transmembrane proteins that mediate the cellular uptake and intracellular trafficking of nucleic acids, playing important roles in the immune response and tumorigenesis. Previous work has suggested that human SIDT1 and SIDT2 are N-glycosylated, but the precise site-specific N-glycosylation information and its functional contribution remain unclear. In this study, we use high-resolution liquid chromatography tandem mass spectrometry to comprehensively map the N-glycosites and quantify the N-glycosylation profiles of SIDT1 and SIDT2. Further molecular mechanistic probing elucidates the essential role of N-linked glycans in regulating cell surface expression, RNA binding, protein stability, and RNA uptake of SIDT1. Our results provide crucial information about the potential functional impact of N-glycosylation in the regulation of SIDT1-mediated RNA uptake and provide insights into the molecular mechanisms of this promising nucleic acid delivery system with potential implications for therapeutic applications. © 2024 The Authors LA - English DB - MTMT ER -