Asset Details
Do you wish to reserve the book?
Ets-1 facilitates nuclear entry of NFAT proteins and their recruitment to the IL-2 promoter
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Ets-1 facilitates nuclear entry of NFAT proteins and their recruitment to the IL-2 promoter
Do you wish to request the book?
Ets-1 facilitates nuclear entry of NFAT proteins and their recruitment to the IL-2 promoter
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Ets-1 facilitates nuclear entry of NFAT proteins and their recruitment to the IL-2 promoter
2013
Overview
E26 transformation-specific sequence 1 (Ets-1), the prototype of the ETS family of transcription factors, is critical for the expression of IL-2 by murine Th cells; however, its mechanism of action is still unclear. Here we show that Ets-1 is also essential for optimal production of IL-2 by primary human Th cells. Although Ets-1 negatively regulates the expression of Blimp1, a known suppressor of IL-2 expression, ablation of B lymphocyte-induced maturation protein 1 (Blimp1) does not rescue the expression of IL-2 by Ets-1-deficient Th cells. Instead, Ets-1 physically and functionally interacts with the nuclear factor of activated T-cells (NFAT) and is required for the recruitment of NFAT to the IL-2 promoter. In addition, Ets-1 is located in both the nucleus and cytoplasm of resting Th cells. Nuclear Ets-1 quickly exits the nucleus in response to calcium-dependent signals and competes with NFAT proteins for binding to protein components of noncoding RNA repressor of NFAT complex (NRON), which serves as a cytoplasmic trap for phosphorylated NFAT proteins. This nuclear exit of Ets-1 precedes rapid nuclear entry of NFAT and Ets-1 deficiency results in impaired nuclear entry, but not dephosphorylation, of NFAT proteins. Thus, Ets-1 promotes the expression of IL-2 by modulating the activity of NFAT.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Humans
/ Interleukin-2 - biosynthesis
/ Mice
/ Multiprotein Complexes - metabolism
/ NFATC Transcription Factors - metabolism
/ Positive Regulatory Domain I-Binding Factor 1
/ Proteins
/ Proto-Oncogene Protein c-ets-1 - deficiency
/ Proto-Oncogene Protein c-ets-1 - metabolism
/ RNA
/ Transcription Factors - deficiency
