ArticleMolecular biology of the cell2016
Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 92 citations in OpenAlex.
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- Orphan quality control by an SCF ubiquitin ligase directed to pervasive C-degrons.Nature communications · 2023Article
- Redundancy and the role of protein copy numbers in the cell polarization machinery of budding yeast.Nature communications · 2023Article
- Molecular mechanism for activation of the 26S proteasome by ZFAND5.Molecular cell · 2023Article
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- Revisiting degron motifs in human AURKA required for its targeting by APC/CLife science alliance · 2023Article
- Relative Protein Lifetime Measurement in Plants Using Tandem Fluorescent Protein Timers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Application of anEngineering in life sciences · 2023Article
- Variation in ubiquitin system genes creates substrate-specific effects on proteasomal protein degradation.eLife · 2022Article
- Review
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Corrections and comments
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Authors and funding
9 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tandem fluorescent protein timers (tFTs) report on protein age through time-dependent change in color, which can be exploited to study protein turnover and trafficking. Each tFT, composed of two fluorescent proteins (FPs) that differ in maturation kinetics, is suited to follow protein dynamics within a specific time range determined by the maturation rates of both FPs. So far, tFTs have been constructed by combining slower-maturing red fluorescent proteins (redFPs) with the faster-maturing superfolder green fluorescent protein (sfGFP). Toward a comprehensive characterization of tFTs, we compare here tFTs composed of different faster-maturing green fluorescent proteins (greenFPs) while keeping the slower-maturing redFP constant (mCherry). Our results indicate that the greenFP maturation kinetics influences the time range of a tFT. Moreover, we observe that commonly used greenFPs can partially withstand proteasomal degradation due to the stability of the FP fold, which results in accumulation of tFT fragments in the cell. Depending on the order of FPs in the timer, incomplete proteasomal degradation either shifts the time range of the tFT toward slower time scales or precludes its use for measurements of protein turnover. We identify greenFPs that are efficiently degraded by the proteasome and provide simple guidelines for the design of new tFTs.
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