Importance of the Conserved Carboxyl-Terminal CNOT1 Binding Domain to Tristetraprolin Activity In Vivo

Author:

Lai Wi S.1,Stumpo Deborah J.1,Wells Melissa L.1,Gruzdev Artiom2,Hicks Stephanie N.1,Nicholson Cindo O.1,Yang Zhengfeng34,Faccio Roberta34,Webster Michael W.5,Passmore Lori A.5,Blackshear Perry J.16

Affiliation:

1. Signal Transduction Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina, USA

2. Reproductive & Developmental Biology Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina, USA

3. Department of Orthopaedic Surgery, Washington University School of Medicine, St. Louis, Missouri, USA

4. Shriners Hospitals for Children, St. Louis, Missouri, USA

5. MRC Laboratory of Molecular Biology, Cambridge, United Kingdom

6. Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, North Carolina, USA

Abstract

Tristetraprolin (TTP) is an anti-inflammatory protein that modulates the stability of certain cytokine/chemokine mRNAs. After initial high-affinity binding to AU-rich elements in 3′ untranslated regions of target mRNAs, mediated through its tandem zinc finger (TZF) domain, TTP promotes the deadenylation and ultimate decay of target transcripts.

Funder

Intramural Research Program of the NIH, NIEHS

HHS | National Institutes of Health

RCUK | Medical Research Council

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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