The proteasome is the central protease in generating peptide repertoires for antigen presentation on human leukocyte antigen class I (HLA-I). Proteasomes not only can catalyze peptide hydrolysis but are also capable of mediating transpeptidation, resulting in spliced peptides generation, a process known as proteasome-catalyzed peptide splicing (PCPS). Despite its immunological importance, it is still unclear what are the determinants of PCPS that favor transpeptidation over hydrolysis. Hence, we sought to characterize the processing of many protein substrates and their peptide products by using a simplistic in vitro antigen processing system and analyzed by mass spectrometry followed by a refined downstream data analysis pipeline.
[doi:10.25345/C5X921V5S]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Mass Spectrometry ; antigen processing ; 20S proteasomes ; MHC-I presentation
Principal Investigators: (in alphabetical order) |
Dr. Juliane Liepe, Max Planck Institute for Multidisciplinary Sciences, Germany Michele Mishto, King's College London and the Francis Crick Institute, United Kingdom |
Submitting User: | waitucksoh |
Wai Tuck Soh, Hanna P. Roetschke, John A. Cormican, Bei Fang Teo, Nyet Cheng Chiam, Monika Raabe, Ralf Pflanz, Fabian Henneberg, Stefan Becker, Ashwin Chari, Haiyan Liu, Henning Urlaub, Juliane Liepe & Michele Mishto.
Protein degradation by human 20S proteasomes elucidates the interplay between peptide hydrolysis and splicing.
Soh, W.T., Roetschke, H.P., Cormican, J.A. et al. Protein degradation by human 20S proteasomes elucidates the interplay between peptide hydrolysis and splicing. Nat Commun 15, 1147 (2024). https://doi.org/10.1038/s41467-024-45339-3.
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