ZFP36

ZFP36
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4J8S
Identifiers
Aliases	ZFP36, G0S24, GOS24, NUP475, RNF162A, TIS11, TTP, zfp-36, ZFP36 ring finger protein
External IDs	MGI: 99180 HomoloGene: 2558 GeneCards: ZFP36
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	39,409,412 bp[1]
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)[2]
End	28,380,253 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• DNA binding; • C-C chemokine binding; • 14-3-3 protein binding; • AU-rich element binding; • metal ion binding; • protein binding; • single-stranded RNA binding; • mRNA 3'-UTR AU-rich region binding; • enzyme binding; • mRNA binding; • protein kinase binding; • RNA binding; • heat shock protein binding; • RNA polymerase binding;
Cellular component	• cytoplasm; • cytoplasmic stress granule; • cell nucleus; • RISC-loading complex; • Ribonucleoprotein; • Dcp1-Dcp2 complex; • exosome (RNase complex); • P-body; • cytosol; • CCR4-NOT complex; • intracellular ribonucleoprotein complex;
Biological process	• nuclear-transcribed mRNA poly(A) tail shortening; • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; • mRNA catabolic process; • regulation of tumor necrosis factor production; • negative regulation of transcription from RNA polymerase II promoter; • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; • miRNA mediated inhibition of translation; • response to starvation; • 3'-UTR-mediated mRNA stabilization; • negative regulation of erythrocyte differentiation; • cellular response to lipopolysaccharide; • cellular response to tumor necrosis factor; • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; • positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA; • regulation of keratinocyte apoptotic process; • regulation of keratinocyte proliferation; • positive regulation of fat cell differentiation; • cellular response to fibroblast growth factor stimulus; • cellular response to granulocyte macrophage colony-stimulating factor stimulus; • negative regulation of viral transcription; • regulation of keratinocyte differentiation; • negative regulation of interleukin-2 biosynthetic process; • response to wounding; • positive regulation of gene silencing by miRNA; • regulation of mRNA stability; • MAPK cascade; • cellular response to glucocorticoid stimulus; • cellular response to epidermal growth factor stimulus; • positive regulation of intracellular mRNA localization; • p38MAPK cascade; • nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; • gene silencing by RNA; • mRNA transport; • 3'-UTR-mediated mRNA destabilization; • negative regulation of polynucleotide adenylyltransferase activity; • transport;
	Sources:Amigo / QuickGO
Orthologs
	7538
	22695
	ENSG00000128016
	ENSMUSG00000044786
	P26651
	P22893
	NM_003407
	NM_011756
	NP_003398
	NP_035886
	Wikidata
View/Edit Human	View/Edit Mouse

Tristetraprolin (TTP), also known as zinc finger protein 36 homolog (ZFP36), is a protein that in humans, mice and rats is encoded by the ZFP36 gene.^[5]^[6] It is a member of the TIS11 (TPA-induced sequence) family, along with butyrate response factors 1 and 2.^[7]

TTP binds to AU-rich elements (AREs) in the 3'-untranslated regions (UTRs) of the mRNAs of some cytokines and promotes their degradation. For example, TTP is a component of a negative feedback loop that interferes with TNF-alpha production by destabilizing its mRNA.^[8] Mice deficient in TTP develop a complex syndrome of inflammatory diseases.^[8]

Interactions

ZFP36 has been shown to interact with 14-3-3 protein family members, such as YWHAH,^[9] and with NUP214, a member of the nuclear pore complex.^[10]

Regulation

Post-transcriptionally, TTP is regulated in several ways.^[7] The subcellular localization of TTP is influenced by interactions with protein partners such as the 14-3-3 family of proteins. These interactions and, possibly, interactions with target mRNAs are affected by the phosphorylation state of TTP, as the protein can be posttranslationally modified by a large number of protein kinases.^[7] There is some evidence that the TTP transcript may also be targeted by microRNAs, such as miR-29a.^[7]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000128016 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000044786 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ DuBois RN, McLane MW, Ryder K, Lau LF, Nathans D (Dec 1990). "A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence". J Biol Chem. 265 (31): 19185–91. PMID 1699942.
↑ "Entrez Gene: ZFP36 zinc finger protein 36, C3H type, homolog (mouse)".
1 2 3 4 Sanduja S, Blanco FF, Dixon DA (2011). "The roles of TTP and BRF proteins in regulated mRNA decay". Wiley Interdiscip Rev RNA. 2 (1): 42–57. doi:10.1002/wrna.28. PMC 3030256. PMID 21278925.
1 2 Carballo E, Lai WS, Blackshear PJ (August 1998). "Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin". Science. 281 (5379): 1001–5. doi:10.1126/science.281.5379.1001. PMID 9703499.
↑ Johnson BA, Stehn JR, Yaffe MB, Blackwell TK (May 2002). "Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms". J. Biol. Chem. 277 (20): 18029–36. doi:10.1074/jbc.M110465200. PMID 11886850.
↑ Carman JA, Nadler SG (March 2004). "Direct association of tristetraprolin with the nucleoporin CAN/Nup214". Biochem. Biophys. Res. Commun. 315 (2): 445–9. doi:10.1016/j.bbrc.2004.01.080. PMID 14766228.

Blackshear PJ (2003). "Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover". Biochem. Soc. Trans. 30 (Pt 6): 945–52. doi:10.1042/bst0300945. PMID 12440952.
Carrick DM, Lai WS, Blackshear PJ (2005). "The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis". Arthritis Research & Therapy. 6 (6): 248–64. doi:10.1186/ar1441. PMC 1064869. PMID 15535838.
Taylor GA, Lai WS, Oakey RJ, et al. (1991). "The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes". Nucleic Acids Res. 19 (12): 3454. doi:10.1093/nar/19.12.3454. PMC 328350. PMID 2062660.
Lai WS, Stumpo DJ, Blackshear PJ (1990). "Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein". J. Biol. Chem. 265 (27): 16556–63. PMID 2204625.
Taylor GA, Thompson MJ, Lai WS, Blackshear PJ (1995). "Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro". J. Biol. Chem. 270 (22): 13341–7. doi:10.1074/jbc.270.22.13341. PMID 7768935.
Heximer SP, Forsdyke DR (1993). "A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor". DNA Cell Biol. 12 (1): 73–88. doi:10.1089/dna.1993.12.73. PMID 8422274.
Huebner K, Druck T, LaForgia S, et al. (1993). "Chromosomal localization of four human zinc finger cDNAs". Hum. Genet. 91 (3): 217–22. doi:10.1007/BF00218259. PMID 8478004.
Lai WS, Carballo E, Thorn JM, et al. (2000). "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. 275 (23): 17827–37. doi:10.1074/jbc.M001696200. PMID 10751406.
Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences". J. Biol. Chem. 277 (9): 7021–8. doi:10.1074/jbc.M108417200. PMID 11748221.
Lai WS, Kennington EA, Blackshear PJ (2002). "Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs". J. Biol. Chem. 277 (11): 9606–13. doi:10.1074/jbc.M110395200. PMID 11782475.
Johnson BA, Stehn JR, Yaffe MB, Blackwell TK (2002). "Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms". J. Biol. Chem. 277 (20): 18029–36. doi:10.1074/jbc.M110465200. PMID 11886850.
Brooks SA, Connolly JE, Diegel RJ, et al. (2002). "Analysis of the function, expression, and subcellular distribution of human tristetraprolin". Arthritis Rheum. 46 (5): 1362–70. doi:10.1002/art.10235. PMID 12115244.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Amann BT, Worthington MT, Berg JM (2003). "A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure". Biochemistry. 42 (1): 217–21. doi:10.1021/bi026988m. PMID 12515557.
Yu H, Stasinopoulos S, Leedman P, Medcalf RL (2003). "Inherent instability of plasminogen activator inhibitor type 2 mRNA is regulated by tristetraprolin". J. Biol. Chem. 278 (16): 13912–8. doi:10.1074/jbc.M213027200. PMID 12578825.
Sawaoka H, Dixon DA, Oates JA, Boutaud O (2003). "Tristetraprolin binds to the 3'-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site". J. Biol. Chem. 278 (16): 13928–35. doi:10.1074/jbc.M300016200. PMID 12578839.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000128016 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000044786 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid1699942-5] DuBois RN, McLane MW, Ryder K, Lau LF, Nathans D (Dec 1990). "A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence". J Biol Chem. 265 (31): 19185–91. PMID 1699942.

[entrez-6] "Entrez Gene: ZFP36 zinc finger protein 36, C3H type, homolog (mouse)".

[pmid21278925-7] 1 2 3 4 Sanduja S, Blanco FF, Dixon DA (2011). "The roles of TTP and BRF proteins in regulated mRNA decay". Wiley Interdiscip Rev RNA. 2 (1): 42–57. doi:10.1002/wrna.28. PMC 3030256. PMID 21278925.

[pmid9703499-8] 1 2 Carballo E, Lai WS, Blackshear PJ (August 1998). "Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin". Science. 281 (5379): 1001–5. doi:10.1126/science.281.5379.1001. PMID 9703499.

[pmid11886850-9] Johnson BA, Stehn JR, Yaffe MB, Blackwell TK (May 2002). "Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms". J. Biol. Chem. 277 (20): 18029–36. doi:10.1074/jbc.M110465200. PMID 11886850.

[pmid14766228-10] Carman JA, Nadler SG (March 2004). "Direct association of tristetraprolin with the nucleoporin CAN/Nup214". Biochem. Biophys. Res. Commun. 315 (2): 445–9. doi:10.1016/j.bbrc.2004.01.080. PMID 14766228.

ZFP36

Interactions

Regulation

References

Further reading