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• W2103174614 startingPage "2865" @default.
• W2103174614 abstract "Elf-1, a member of the E 26-specific transcription factor family with a predicted molecular mass of 68 kDa, is involved in the transcriptional regulation of several hematopoietic cell genes. We demonstrate that Elf-1 exists primarily as a 98-kDa form in the nucleus and as an 80-kDa form in the cytoplasm. Phosphorylation and O-linked glycosylation contribute to the increased posttranslational molecular mass of Elf-1. The 98-kDa Elf-1 is released from the cytoplasm tethering retinoblastoma protein and moves to the nucleus, where it binds to the promoter of the TCR zeta-chain gene. Finally, the cytoplasmic 98-kDa form enters the proteasome pathway and undergoes degradation. In conclusion, different forms of Elf-1 are the products of posttranslational modifications that determine its subcellular localization, activity, and metabolic degradation." @default.
• W2103174614 created "2016-06-24" @default.
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• W2103174614 date "2002-03-15" @default.
• W2103174614 modified "2023-10-14" @default.
• W2103174614 title "Phosphorylation and <i>O</i>-Linked Glycosylation of Elf-1 Leads to Its Translocation to the Nucleus and Binding to the Promoter of the TCR ζ-Chain" @default.
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• W2103174614 doi "https://doi.org/10.4049/jimmunol.168.6.2865" @default.
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