ArticleMolecular bioSystems2014
A FRET-based approach for identification of proteasome catalytic subunit composition.
Article in Molecular bioSystems, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Site-Specific Proteasome Inhibitors.Biomolecules · 2021Review
- Fluorescent Probes with Unnatural Amino Acids to Monitor Proteasome Activity in Real-Time.ACS chemical biology · 2020Article
- H727 cells are inherently resistant to the proteasome inhibitor carfilzomib, yet require proteasome activity for cell survival and growth.Scientific reports · 2019Article
- Highlighting the Proteasome: Using Fluorescence to Visualize Proteasome Activity and Distribution.Frontiers in molecular biosciences · 2019Review
- Polymer micelle formulation for the proteasome inhibitor drug carfilzomib: Anticancer efficacy and pharmacokinetic studies in mice.PloS one · 2017Article
- Elucidating the catalytic subunit composition of distinct proteasome subtypes: a crosslinking approach employing bifunctional activity-based probes.Chembiochem : a European journal of chemical biology · 2015Article
- Modelling proteasome and proteasome regulator activities.Biomolecules · 2014Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Mammalian cells have two main types of proteasomes, the constitutive proteasome and the immunoproteasome, each containing a distinct set of three catalytic subunits. Recently, additional proteasome subtypes containing a non-standard mixture of catalytic subunits have gained increasing attention, especially due to their presence in cancer settings. However, practical methods for identifying proteasome subtypes have been lacking. Here, we report the development of the first fluorescence resonance energy transfer (FRET)-based strategy that can be utilized to identify different proteasome subtypes present within cells. We have developed FRET donor- and acceptor-probes that are based on previously reported peptide epoxyketones and selectively target individual proteasome catalytic subunits. Using the purified proteasome and cancer cell lysates, we demonstrate the feasibility of a FRET-based approach for determining the catalytic subunit composition of individual 20S proteasome subtypes. Ultimately, this approach may be utilized to study the functions of individual proteasome subtypes in cells.
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Registered trials
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