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The Journal of Immunology, 2002, 168: 2865-2871.
Copyright © 2002 by The American Association of Immunologists

Phosphorylation and O-Linked Glycosylation of Elf-1 Leads to Its Translocation to the Nucleus and Binding to the Promoter of the TCR {zeta}-Chain1

Yuang-Taung Juang*,{dagger}, Elena E. Solomou*,{dagger}, Barbara Rellahan{ddagger} and George C. Tsokos2,*,{dagger}

* Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814; {dagger} Department of Cellular Injury, Walter Reed Army Institute of Research, Silver Spring, MD 20910; and {ddagger} Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892

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.




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