mRNA decay activator protein ZFP36

Definition:

Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation. Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self regulates by destabilizing its own mRNA. Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages (By similarity). Also plays a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia. Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (By similarity). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA (By similarity). Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs. Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs. May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing (By similarity). Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages (By similarity). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (By similarity). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells.; (Microbial infection) Negatively regulates HTLV-1 TAX-dependent transactivation of viral long terminal repeat (LTR) promoter.

References:

[1]. Frauke Prenzler, et al. Functional analysis of ZFP36 proteins in keratinocytes. Eur J Cell Biol. 2016 Aug;95(8):277-84. [Content Brief]

[2]. Qing Jing, et al. Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell. 2005 Mar 11;120(5):623-34. [Content Brief]

[3]. C Y Chen, et al. AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell. 2001 Nov 16;107(4):451-64. [Content Brief]

[4]. Thierry J Horner, et al. Stimulation of polo-like kinase 3 mRNA decay by tristetraprolin. Mol Cell Biol. 2009 Apr;29(8):1999-2010. [Content Brief]

[5]. Melissa A Hausburg, et al. Post-transcriptional regulation of satellite cell quiescence by TTP-mediated mRNA decay. Elife. 2015 Mar 27;4:e03390. [Content Brief]

[6]. E Carballo, et al. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science. 1998 Aug 14;281(5379):1001-5. [Content Brief]

[7]. Martin Fenger-Grøn, et al. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell. 2005 Dec 22;20(6):905-15. [Content Brief]

[8]. Daniel Peter, et al. Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression. Genes Dev. 2019 Oct 1;33(19-20):1355-1360. [Content Brief]

[9]. Seth A Brooks, et al. Analysis of the function, expression, and subcellular distribution of human tristetraprolin. Arthritis Rheum. 2002 May;46(5):1362-70. [Content Brief]

[10]. Tobias M Franks, et al. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 2007 Mar 15;21(6):719-35. [Content Brief]

[11]. Rachel L Ogilvie, et al. Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay. J Immunol. 2005 Jan 15;174(2):953-61. [Content Brief]

[12]. Marc R Fabian, et al. Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin. Nat Struct Mol Biol. 2013 Jun;20(6):735-9. [Content Brief]

[13]. Vishram P Kedar, et al. Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85. PLoS One. 2010 Mar 8;5(3):e9588. [Content Brief]

[14]. Shannon L Nowotarski, et al. Destabilization of the ornithine decarboxylase mRNA transcript by the RNA-binding protein tristetraprolin. Amino Acids. 2016 Oct;48(10):2303-11. [Content Brief]

[15]. Jillian Emmons, et al. Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation. RNA. 2008 May;14(5):888-902. [Content Brief]

[16]. Sandrine Chamboredon, et al. Hypoxia-inducible factor-1α mRNA: a new target for destabilization by tristetraprolin in endothelial cells. Mol Biol Cell. 2011 Sep;22(18):3366-78. [Content Brief]

[17]. Jens Lykke-Andersen, et al. Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev. 2005 Feb 1;19(3):351-61. [Content Brief]

[18]. Wi S Lai, et al. Novel mRNA targets for tristetraprolin (TTP) identified by global analysis of stabilized transcripts in TTP-deficient fibroblasts. Mol Cell Biol. 2006 Dec;26(24):9196-208. [Content Brief]

[19]. Liangqian Huang, et al. Interaction with Pyruvate Kinase M2 Destabilizes Tristetraprolin by Proteasome Degradation and Regulates Cell Proliferation in Breast Cancer. Sci Rep. 2016 Mar 1;6:22449. [Content Brief]

[20]. M Marderosian, et al. Tristetraprolin regulates Cyclin D1 and c-Myc mRNA stability in response to rapamycin in an Akt-dependent manner via p38 MAPK signaling. Oncogene. 2006 Oct 12;25(47):6277-90. [Content Brief]

[21]. Jean-Claude Twizere, et al. Interaction of retroviral Tax oncoproteins with tristetraprolin and regulation of tumor necrosis factor-alpha expression. J Natl Cancer Inst. 2003 Dec 17;95(24):1846-59. [Content Brief]

[22]. Tatiana Vignudelli, et al. ZFP36L1 negatively regulates erythroid differentiation of CD34+ hematopoietic stem cells by interfering with the Stat5b pathway. Mol Biol Cell. 2010 Oct 1;21(19):3340-51. [Content Brief]

[23]. Wi S Lai, et al. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol Cell Biol. 2003 Jun;23(11):3798-812. [Content Brief]

[24]. W S Lai, et al. Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA. Mol Cell Biol. 1999 Jun;19(6):4311-23. [Content Brief]

[25]. W S Lai, et al. Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA. J Biol Chem. 2000 Jun 9;275(23):17827-37. [Content Brief]

[26]. W S Lai, et al. Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-mediated AU-rich element-dependent mRNA degradation can occur in the absence of a poly(A) tail. J Biol Chem. 2001 Jun 22;276(25):23144-54. [Content Brief]

[27]. Seth A Brooks, et al. The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. J Immunol. 2004 Jun 15;172(12):7263-71. [Content Brief]

Biomedical Dictionary

The Biomedical Dictionary is a comprehensive and professional collection of biological academic terms and subject datas. All explanations are supported by authoritative books or high impact factor literatures, and you can acquire accurate explanations of the biomedical terms you want to know.

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z #

Name
Email *

	Sorry, but the email address you supplied was invalid.