Abstract
The Ets1 proto-oncoprotein is a member of the Ets family of transcription factors that share a unique DNA binding domain, the Ets domain. The DNA binding activity of Ets1 is controlled by kinases and transcription factors. Some transcription factors, such as AML-1, regulate Ets1 by targeting its autoinhibitory module. Others, such as Pax-5, alter Ets1 DNA binding properties. Ets1 harbors two phosphorylation sites, threonine-38 and an array of serines within the exon VII domain. Phosphorylation of threonine-38 by ERK1/2 activates Ets1, whereas phosphorylation of the exon VII domain by CaMKII or MLCK inhibits Ets1 DNA binding activity. Ets1 is expressed by numerous cell types. In haemotopoietic cells, it contributes to the regulation of cellular differentiation. In a variety of other cells, including endothelial cells, vascular smooth muscle cells and epithelial cancer cells, Ets1 promotes invasive behavior. Regulation of MMP1, MMP3, MMP9 and uPA as well as of VEGF and VEGF receptor gene expression has been ascribed to Ets1. In tumors, Ets1 expression is indicative of poorer prognosis.
Highlights
Ets proteins comprise a family of transcription factors that share a unique DNA binding domain, the Ets domain [1,2,3,4]
Ets1 is important for mediating transcriptional activation of specific genes by the transforming viral protein Tax, a transactivator that is encoded by the region X of the human T-cell lymphotropic virus I (HTLV-I)
Ets1 seems to participate in the regulation of invasive behavior of many normal and tumor cells alike
Summary
Ets proteins comprise a family of transcription factors that share a unique DNA binding domain, the Ets domain [1,2,3,4]. The c-ets locus contains two different start sites leading to the expression of p68c-ets and p54c-ets. The c-ets locus contains two different start sites leading to the expression of p68c-ets and p54c-ets1 These two proteins differ in their N-terminal sequence [14]. The Ets domain recognizes DNA sequences that contain a GGAA/T core element [19]. The distantly related Ets factor PU. binds in a similar way to DNA [21] demonstrating that the Ets domain/DNA interaction is highly preserved. Ets proteins differ significantly in their preference for the sequence flanking the GGAA/T core motif.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
