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• W2118721386 abstract "MrfA, a transcription factor that regulates Dictyostelium prestalk cell differentiation, is an orthologue of the metazoan myelin gene regulatory factor (MRF) proteins. We show that the MRFs contain a predicted transmembrane domain, suggesting that they are synthesised as membrane-tethered proteins that are then proteolytically released. We confirm this for MrfA but report a radically different mode of processing from that of paradigmatic tethered transcriptional regulators, which are cleaved within the transmembrane domain by a dedicated protease. Instead, an auto-proteolytic cleavage mechanism, previously only described for the intramolecular chaperone domains of bacteriophage tail-spike proteins, processes MrfA and, by implication, the metazoan MRF proteins. We also present evidence that the auto-proteolysis of MrfA occurs rapidly and constitutively in the ER and that its specific role in prestalk cell differentiation is conferred by the regulated nuclear translocation of the liberated fragment." @default.
• W2118721386 created "2016-06-24" @default.
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• W2118721386 date "2013-01-01" @default.
• W2118721386 modified "2023-10-01" @default.
• W2118721386 title "A new kind of membrane-tethered eukaryotic transcription factor that shares an auto-proteolytic processing mechanism with bacteriophage tail-spike proteins" @default.
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• W2118721386 doi "https://doi.org/10.1242/jcs.133231" @default.
• W2118721386 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3828593" @default.
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