Disease relevance of ZFP36L1

• Erk mediates this induction of Brf1 expression and therefore contributes in at least two ways to pol III transcriptional activation during hypertrophy [1].
• In addition, we demonstrate that large T antigen can cofractionate and coimmunoprecipitate with the hBRF-containing complex TFIIIB derived from HeLa cells infected with a recombinant adenovirus which expresses large T antigen [2].
• Butyrate response factor 1 enhances cisplatin sensitivity in human head and neck squamous cell carcinoma cell lines [3].
• The authors report the identification of 2 cell membrane-permeable compounds that exhibit activity in the ERF1 Redistribution assay and selectively inhibit proliferation of MAPK pathway-dependent malignant melanoma cells at similar potencies (IC(50)=< 5 microM) [4].
• These included up-regulation of butyrate response factor 1 (BRF1) and down-regulation of c-jun and the breast cancer associated ring domain gene known as BARD1 [5].

High impact information on ZFP36L1

• The accumulation of ARE-mRNAs in PBs is strongly enhanced when the mRNA decay machinery is rendered limiting by mRNA decay enzyme depletion or TTP/BRF-1 overexpression [6].
• Furthermore, hypertrophic stimulation increases expression of the essential TFIIIB subunit Brf1, an effect not seen when fibroblasts proliferate [1].
• Finally, we show that arsenite promotes the delayed association of PMR1 with SGs under conditions which cause tristetraprolin and butyrate response factor 1, proteins that facilitate exonucleolytic mRNA, to exit SGs [7].
• However, IL-4 did protect Ramos cells from apoptosis induced by calcium ionophore and this effect was accompanied by inhibition of ionophore-induced expression of an immediate early gene encoding a 36-kDa zinc-finger protein, Berg36 [8].
• It was shown that the LTR sequences of two subfamilies harbor a specific binding site for a complex consisting of at least three proteins, ERF1, ERF2 and ERF3 of 98, 91 and 88 kDa apparent molecular mass, respectively [9].

Biological context of ZFP36L1

• We have used macroarrays to identify zinc finger protein butyrate response factor-1 (BRF1) as a novel PTH regulated gene in clonal and normal osteoblasts of human and rodent origin [10].
• Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1 [11].
• Distinct mechanisms for rescue from apoptosis in Ramos human B cells by signalling through CD40 and interleukin-4 receptor: role for inhibition of an early response gene, Berg36 [12].
• Fragments encoding the middle portion and the 3' end were discovered in the Bombyx mori Genome Project "Silkbase" collection through sequence homology with human BRF1, and the fragment encoding the N-terminus was isolated in our laboratory using the 5' RACE method [13].

Anatomical context of ZFP36L1

• In mouse calvarial osteoblasts, BRF1 mRNA levels are upregulated by PTH(1-84) and reduced in response to bone morphogenetic protein 2 (BMP-2) [10].

Associations of ZFP36L1 with chemical compounds

• Two other short-chain fatty acids, propionate and acetate, have no detectable effects on BRF1 or BRF2 transcription [14].

Other interactions of ZFP36L1

• Our initial data demonstrated that the immediate-early gene butyrate response factor 1 ( BRF1) was upregulated in HTLV-1-infected cells [15].

References