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research
The basic helix loop helix transcription factor twist1 is a novel regulator of ATF4 in osteoblasts
Authors
Ardura
Bellido
+40 more
Bialek
Boudreaux
Burgess
Chaudhary
Chen
Chen
Connerney
Danciu
Datta
Ducy
Ducy
Ducy
Ducy
Frendo
Gardella
Iida-Klein
Jiang
Jilka
Komori
Krishnan
Li
Liao
Makarova
McCabe
McCauley
Miao
Muir
Mundlos
Nakashima
Pettway
Schmidt
Sosic
Suzuki
Wang
Xiao
Yang
Yang
Yu
Yu
Yu
Publication date
1 January 2012
Publisher
'Wiley'
Doi
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on
PubMed
Abstract
Parathyroid hormone (PTH) is an essential regulator of endochondral bone formation and an important anabolic agent for the reversal of bone loss. PTH mediates its functions in part by regulating binding of the bone‐related activating transcription factor 4 (ATF4) to the osteoblast‐specific gene, osteocalcin. The basic helix‐loop‐helix (bHLH) factors Twist1 and Twist2 also regulate osteocalcin transcription in part through the interaction of the C‐terminal “box” domain in these factors and Runx2. In this study, we discovered a novel function of PTH: its ability to dramatically decrease Twist1 transcription. Since ATF4 is a major regulator of the PTH response in osteoblasts, we assessed the mutual regulation between these factors and determined that Twist proteins and ATF4 physically interact in a manner that affects ATF4 DNA binding function. We mapped the interaction domain of Twist proteins to the C‐terminal “box” domain and of ATF4, to the N‐terminus. Furthermore, we demonstrate that Twist1 overexpression in osteoblasts attenuates ATF4 binding to the osteocalcin promoter in response to PTH. This study thus identifies Twist proteins as novel inhibitory binding partners of ATF4 and explores the functional significance of this interaction. J. Cell. Biochem. 113: 70–79, 2012. © 2011 Wiley Periodicals, Inc.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/89496/1/23329_ftp.pd
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info:doi/10.1002%2Fjcb.23329
Last time updated on 02/01/2020
Deep Blue Documents at the University of Michigan
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Last time updated on 25/05/2012