HuR binds to a single site on the C/EBP - beta mRNA of 3T3-L1 Adipocytes
Author
Jones, Heath; Carver, Melinda; Pekala, Phillip H.
Abstract
HuR is a ligand for nuclear mRNAs containing adenylate-uridylate rich elements in the 3'- untranslated region. Once bound to the mRNA, HuR is recognized by adapter proteins which then facilitate nuclear export of the complex. In the cytosol HuR is thought to function to control stability and translation of its ligand message. In the 3T3-L1 cells HuR is constitutively expressed and localized predominantly to the nucleus in the preadipocytes. However within 30 min of exposure to
the differentiation stimulus, the HuR content in the cytosol increases consistent with HuR regulating the availability of relevant mRNAs for translation. Using in vitro RNA gel shifts, we have demonstrated that the C/EBPß message is a ligand for HuR and that the single binding site is an adenylate-uridylate rich element in the 3'untranslated region. Originally published Biochemical and Biophysical Research Communications, Vol. 355, No. 1, Mar 2007
Date
2007-03-30
Citation:
APA:
Jones, Heath, & Carver, Melinda, & Pekala, Phillip H.. (March 2007).
HuR binds to a single site on the C/EBP - beta mRNA of 3T3-L1 Adipocytes.
Biochemical and Biophysical Research Communications,
355(1),
217-
220. Retrieved from
http://hdl.handle.net/10342/3315
MLA:
Jones, Heath, and Carver, Melinda, and Pekala, Phillip H..
"HuR binds to a single site on the C/EBP - beta mRNA of 3T3-L1 Adipocytes". Biochemical and Biophysical Research Communications.
355:1. (217-220),
March 2007.
October 03, 2023.
http://hdl.handle.net/10342/3315.
Chicago:
Jones, Heath and Carver, Melinda and Pekala, Phillip H.,
"HuR binds to a single site on the C/EBP - beta mRNA of 3T3-L1 Adipocytes," Biochemical and Biophysical Research Communications 355, no.
1 (March 2007),
http://hdl.handle.net/10342/3315 (accessed
October 03, 2023).
AMA:
Jones, Heath, Carver, Melinda, Pekala, Phillip H..
HuR binds to a single site on the C/EBP - beta mRNA of 3T3-L1 Adipocytes. Biochemical and Biophysical Research Communications.
March 2007;
355(1):
217-220.
http://hdl.handle.net/10342/3315. Accessed
October 03, 2023.
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Publisher
East Carolina University