Asset Details
Do you wish to reserve the book?
Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation
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?
Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation
Do you wish to request the book?
Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation
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
Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation
2006
Overview
We have previously shown that interferon regulatory factor-2 (IRF-2) is acetylated in a cell growth-dependent manner, which enables it to contribute to the transcription of cell growth-regulated promoters. To clarify the function of acetylation of IRF-2, we investigated the proteins that associate with acetylated IRF-2. In 293T cells, the transfection of p300/CBP-associated factor (PCAF) enhanced the acetylation of IRF-2. In cells transfected with both IRF-2 and PCAF, IRF-2 associated with endogenous nucleolin, while in contrast, minimal association was observed when IRF-2 was transfected with a PCAF histone acetyl transferase (HAT) deletion mutant. In a pull-down experiment using stable transfectants, acetylation-defective mutant IRF-2 (IRF-2K75R) recruited nucleolin to a much lesser extent than wild-type IRF-2, suggesting that nucleolin preferentially associates with acetylated IRF-2. Nucleolin in the presence of PCAF enhanced IRF-2-dependent
H4
promoter activity in NIH3T3 cells. Nucleolin knock-down using siRNA reduced the IRF-2/PCAF-mediated promoter activity. Chromatin immunoprecipitation analysis indicated that PCAF transfection increased nucleolin binding to IRF-2 bound to the
H4
promoter. We conclude that nucleolin is recruited to acetylated IRF-2, thereby contributing to gene regulation crucial for the control of cell growth.
Publisher
Springer Science and Business Media LLC,Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
/ Animals
/ Biological and medical sciences
/ Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
/ Fundamental and applied biological sciences. Psychology
/ Genetics
/ Histone Acetyltransferases - genetics
/ Histones
/ Humans
/ Interferon regulatory factor
/ Interferon Regulatory Factor-2
/ Interferon Regulatory Factor-2 - genetics
/ Interferon Regulatory Factor-2 - physiology
/ Medicine
/ Mice
/ Molecular and cellular biology
/ Mutation
/ Oncology
/ p300-CBP Transcription Factors
/ p300-CBP Transcription Factors - genetics
/ p300-CBP Transcription Factors - physiology
/ Phosphoproteins - physiology
/ Proteins
/ Recombinant Proteins - metabolism
/ RNA-Binding Proteins - physiology
/ siRNA
