Perry Justin Blackshear

Journal article Nat Commun · August 13, 2025 Tristetraprolin family of proteins regulate mRNA stability by binding to specific AU-rich elements in transcripts. This binding promotes the shortening of the mRNA poly(A) tail, or deadenylation, initiating mRNA degradation. The CCR4-NOT complex plays a ce ... Full text Link to item Cite

Synergistic roles of tristetraprolin family members in myeloid cells in the control of inflammation.

Journal article Life Sci Alliance · January 2024 Members of the tristetraprolin (TTP) family of RNA-binding proteins can bind to and promote the decay of specific transcripts containing AU-rich motifs. ZFP36 (TTP) is best known for regulating pro-inflammatory cytokine expression in myeloid cells; however ... Full text Link to item Cite

RNA-Binding Protein-Mediated mRNA Deadenylation in Mammalian Cell Extracts.

Journal article Methods Mol Biol · 2024 Removal of the poly(A) tail, or deadenylation, is a crucial step in destabilizing mRNAs in eukaryotes. In this chapter, we describe a cell-free deadenylation assay that uses cytoplasmic cell extracts from human HEK293 cells transiently transfected with DNA ... Full text Link to item Cite

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

Journal article Mol Cell Biol · July 1, 2019 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 fin ... Full text Link to item Cite

A Knock-In Tristetraprolin (TTP) Zinc Finger Point Mutation in Mice: Comparison with Complete TTP Deficiency.

Journal article Mol Cell Biol · February 15, 2018 Tristetraprolin (TTP) is a tandem CCCH zinc finger protein that can bind to AU-rich element-containing mRNAs and promote their decay. TTP knockout mice develop a severe inflammatory syndrome, largely due to excess tumor necrosis factor (TNF), whose mRNA is ... Full text Link to item Cite

An Ancient Family of RNA-Binding Proteins: Still Important!

Journal article Trends Biochem Sci · April 2017 RNA-binding proteins are important modulators of mRNA stability, a crucial process that determines the ultimate cellular levels of mRNAs and their encoded proteins. The tristetraprolin (TTP) family of RNA-binding proteins appeared early in the evolution of ... Full text Link to item Cite

Tristetraprolin as a Therapeutic Target in Inflammatory Disease.

Journal article Trends Pharmacol Sci · October 2016 Members of the tristetraprolin (TTP) family of RNA-binding proteins are found in all major eukaryotic groups. TTP family members, from plants through humans, can bind adenosine-uridine rich elements in target mRNAs with high affinity. In mammalian cells, t ... Full text Link to item Cite

Effects of Combined Tristetraprolin/Tumor Necrosis Factor Receptor Deficiency on the Splenic Transcriptome.

Journal article Mol Cell Biol · May 2016 Tristetraprolin (TTP) acts by binding to AU-rich elements in certain mRNAs, such as tumor necrosis factor (TNF) mRNA, and increasing their decay rates. TTP knockout mice exhibit a profound inflammatory syndrome that is largely due to increased TNF levels. ... Full text Link to item Cite

Deficiency of the placenta- and yolk sac-specific tristetraprolin family member ZFP36L3 identifies likely mRNA targets and an unexpected link to placental iron metabolism.

Journal article Development · April 15, 2016 The ZFP36L3 protein is a rodent-specific, placenta- and yolk sac-specific member of the tristetraprolin (TTP) family of CCCH tandem zinc finger proteins. These proteins bind to AU-rich elements in target mRNAs, and promote their deadenylation and decay. We ... Full text Link to item Cite

Enhanced stability of tristetraprolin mRNA protects mice against immune-mediated inflammatory pathologies.

Journal article Proc Natl Acad Sci U S A · February 16, 2016 Tristetraprolin (TTP) is an inducible, tandem zinc-finger mRNA binding protein that binds to adenylate-uridylate-rich elements (AREs) in the 3'-untranslated regions (3'UTRs) of specific mRNAs, such as that encoding TNF, and increases their rates of deadeny ... Full text Link to item Cite

Functional equivalence of an evolutionarily conserved RNA binding module.

Journal article J Biol Chem · October 2, 2015 Members of the tristetraprolin (TTP) family of proteins participate in the regulation of mRNA turnover after initially binding to AU-rich elements in target mRNAs. Related proteins from most groups of eukaryotes contain a conserved tandem zinc finger (TZF) ... Full text Link to item Cite

Tristetraprolin (TTP) coordinately regulates primary and secondary cellular responses to proinflammatory stimuli.

Journal article J Leukoc Biol · April 2015 TTP is an anti-inflammatory protein that acts by binding to AREs in its target mRNAs, such as Tnf mRNA, and promoting their deadenylation and decay. TNF released from inflammatory cells can then stimulate gene expression in tissue cells, such as fibroblast ... Full text Link to item Cite

Post-transcriptional regulation of transcript abundance by a conserved member of the tristetraprolin family in Candida albicans.

Journal article Mol Microbiol · March 2015 Members of the tristetraprolin (TTP) family of CCCH tandem zinc finger proteins bind to AU-rich regions in target mRNAs, leading to their deadenylation and decay. Family members in Saccharomyces cerevisiae influence iron metabolism, whereas the single prot ... Full text Link to item Cite

The Drosophila Tis11 protein and its effects on mRNA expression in flies.

Journal article J Biol Chem · December 19, 2014 Members of the mammalian tristetraprolin family of CCCH tandem zinc finger proteins can bind to certain AU-rich elements (AREs) in mRNAs, leading to their deadenylation and destabilization. Mammals express three or four members of this family, but Drosophi ... Full text Link to item Cite

Zfp36l3, a rodent X chromosome gene encoding a placenta-specific member of the Tristetraprolin family of CCCH tandem zinc finger proteins.

Journal article Biol Reprod · August 2005 Members of the tristetraprolin (TTP) family of CCCH tandem zinc finger (TZF) proteins can bind directly to AU-rich elements (ARE) in mRNA, causing deadenylation and destabilization of the transcripts to which they bind. We describe here a novel fourth mamm ... Full text Link to item Cite

Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.

Journal article J Biol Chem · May 30, 2003 Tristetraprolin (TTP) and its two known mammalian family members are tandem CCCH zinc finger proteins that can bind to AU-rich elements (AREs) in cellular mRNAs and destabilize those transcripts, apparently by initiating their deadenylation. Previous studi ... Full text Link to item Cite

Disruption of the gene encoding the mitogen-regulated translational modulator PHAS-I in mice.

Journal article J Biol Chem · December 12, 1997 PHAS-I is the prototype of a group of eIF4E-binding proteins that can regulate mRNA translation in response to hormones and growth factors. To investigate the importance of PHAS-I in the physiology of the intact animal, we disrupted the PHAS-I gene in mice ... Full text Link to item Cite

Tumor-promoting phorbol esters induce angiogenesis in vivo.

Journal article Am J Physiol · February 1988 It has been hypothesized that tumor growth is dependent on the concomitant growth of its vascular supply, and thus agents that stimulate angiogenesis may help support tumor growth. Phorbol esters are potent tumor promoters that induce a variety of biochemi ... Full text Link to item Cite