Hmdb loader
Survey

Showing Protein mRNA decay activator protein ZFP36 (HMDBP13857)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13857
Secondary Accession Numbers None
Name mRNA decay activator protein ZFP36
Synonyms
  1. G0/G1 switch regulatory protein 24
  2. Growth factor-inducible nuclear protein NUP475
  3. Tristetraprolin
  4. Zinc finger protein 36
  5. Zfp-36
Gene Name ZFP36
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function 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 (PubMed:9703499, PubMed:10330172, PubMed:10751406, PubMed:11279239, PubMed:12115244, PubMed:12748283, PubMed:15187101, PubMed:15634918, PubMed:17030620, PubMed:16702957, PubMed:20702587, PubMed:20221403, PubMed:21775632, PubMed:27193233, PubMed:23644599, PubMed:25815583, PubMed:31439631). Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:15687258, PubMed:23644599). Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation (PubMed:23644599). Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs (PubMed:11719186, PubMed:12748283, PubMed:15687258, PubMed:16364915). Self regulates by destabilizing its own mRNA (PubMed:15187101). Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA (PubMed:10330172, PubMed:10751406, PubMed:12115244, PubMed:15187101, PubMed:15634918, PubMed:17030620, PubMed:16702957, PubMed:19188452, PubMed:20702587, PubMed:20221403, PubMed:21775632, PubMed:25815583). 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). Plays also 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 (PubMed:18367721). Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia (PubMed:21775632). 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 (PubMed:20702587). 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 (PubMed:18367721). Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs (PubMed:15766526). May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro (PubMed:16364915). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (PubMed:17369404). 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 (PubMed:27182009). Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (PubMed:26926077).(Microbial infection) Negatively regulates HTLV-1 TAX-dependent transactivation of viral long terminal repeat (LTR) promoter.
Pathways
  • Human T-cell leukemia virus 1 infection
  • Kaposi sarcoma-associated herpesvirus infection
Reactions Not Available
GO Classification
Biological Process
regulation of tumor necrosis factor production
3'-UTR-mediated mRNA destabilization
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
regulation of mRNA stability
cellular response to fibroblast growth factor stimulus
mRNA transport
response to wounding
cellular response to tumor necrosis factor
response to starvation
cellular response to lipopolysaccharide
nuclear-transcribed mRNA poly(A) tail shortening
3'-UTR-mediated mRNA stabilization
cellular response to epidermal growth factor stimulus
miRNA mediated inhibition of translation
negative regulation of transcription from RNA polymerase II promoter
negative regulation of polynucleotide adenylyltransferase activity
negative regulation of viral transcription
negative regulation of erythrocyte differentiation
nuclear-transcribed mRNA catabolic process, deadenylation-independent decay
viral reproduction
p38MAPK cascade
positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA
positive regulation of gene silencing by miRNA
positive regulation of intracellular mRNA localization
positive regulation of nuclear-transcribed mRNA poly(A) tail shortening
regulation of keratinocyte apoptotic process
regulation of keratinocyte proliferation
MAPK cascade
cellular response to granulocyte macrophage colony-stimulating factor stimulus
cellular response to glucocorticoid stimulus
positive regulation of fat cell differentiation
negative regulation of interleukin-2 production
mRNA catabolic process
regulation of keratinocyte differentiation
Cellular Component
cytosol
cytoplasmic mRNA processing body
cytoplasm
nucleus
cytoplasmic stress granule
ribonucleoprotein complex
Molecular Function
protein kinase binding
mRNA 3'-UTR AU-rich region binding
protein-containing complex binding
metal ion binding
heat shock protein binding
RNA binding
RNA polymerase binding
14-3-3 protein binding
C-C chemokine binding
enzyme binding
DNA binding
mRNA binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 332
Molecular Weight 34002.645
Theoretical pI 8.624
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P26651
UniProtKB/Swiss-Prot Entry Name TTP_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  5. Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J: Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol Cell. 2005 Dec 22;20(6):905-15. [PubMed:16364915 ]
  6. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [PubMed:23186163 ]
  7. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569 ]
  8. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [PubMed:21406692 ]
  9. Taylor GA, Lai WS, Oakey RJ, Seldin MF, Shows TB, Eddy RL Jr, Blackshear PJ: The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes. Nucleic Acids Res. 1991 Jun 25;19(12):3454. doi: 10.1093/nar/19.12.3454. [PubMed:2062660 ]
  10. Carballo E, Lai WS, Blackshear PJ: Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science. 1998 Aug 14;281(5379):1001-5. doi: 10.1126/science.281.5379.1001. [PubMed:9703499 ]
  11. Lai WS, Carballo E, Strum JR, Kennington EA, Phillips RS, Blackshear PJ: 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. doi: 10.1128/MCB.19.6.4311. [PubMed:10330172 ]
  12. Lai WS, Carballo E, Thorn JM, Kennington EA, Blackshear PJ: 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. doi: 10.1074/jbc.M001696200. [PubMed:10751406 ]
  13. Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M: AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell. 2001 Nov 16;107(4):451-64. doi: 10.1016/s0092-8674(01)00578-5. [PubMed:11719186 ]
  14. Lai WS, Blackshear PJ: 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. doi: 10.1074/jbc.M100680200. Epub 2001 Mar 28. [PubMed:11279239 ]
  15. Brooks SA, Connolly JE, Diegel RJ, Fava RA, Rigby WF: Analysis of the function, expression, and subcellular distribution of human tristetraprolin. Arthritis Rheum. 2002 May;46(5):1362-70. doi: 10.1002/art.10235. [PubMed:12115244 ]
  16. Twizere JC, Kruys V, Lefebvre L, Vanderplasschen A, Collete D, Debacq C, Lai WS, Jauniaux JC, Bernstein LR, Semmes OJ, Burny A, Blackshear PJ, Kettmann R, Willems L: 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. doi: 10.1093/jnci/djg118. [PubMed:14679154 ]
  17. Lai WS, Kennington EA, Blackshear PJ: 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. doi: 10.1128/MCB.23.11.3798-3812.2003. [PubMed:12748283 ]
  18. Carman JA, Nadler SG: Direct association of tristetraprolin with the nucleoporin CAN/Nup214. Biochem Biophys Res Commun. 2004 Mar 5;315(2):445-9. doi: 10.1016/j.bbrc.2004.01.080. [PubMed:14766228 ]
  19. Brooks SA, Connolly JE, Rigby WF: 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. doi: 10.4049/jimmunol.172.12.7263. [PubMed:15187101 ]
  20. Jing Q, Huang S, Guth S, Zarubin T, Motoyama A, Chen J, Di Padova F, Lin SC, Gram H, Han J: Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell. 2005 Mar 11;120(5):623-34. doi: 10.1016/j.cell.2004.12.038. [PubMed:15766526 ]
  21. Lykke-Andersen J, Wagner E: 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. doi: 10.1101/gad.1282305. [PubMed:15687258 ]
  22. Ogilvie RL, Abelson M, Hau HH, Vlasova I, Blackshear PJ, Bohjanen PR: Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay. J Immunol. 2005 Jan 15;174(2):953-61. doi: 10.4049/jimmunol.174.2.953. [PubMed:15634918 ]
  23. Cao H, Deterding LJ, Venable JD, Kennington EA, Yates JR 3rd, Tomer KB, Blackshear PJ: Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis. Biochem J. 2006 Feb 15;394(Pt 1):285-97. doi: 10.1042/BJ20051316. [PubMed:16262601 ]
  24. Brook M, Tchen CR, Santalucia T, McIlrath J, Arthur JS, Saklatvala J, Clark AR: Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways. Mol Cell Biol. 2006 Mar;26(6):2408-18. doi: 10.1128/MCB.26.6.2408-2418.2006. [PubMed:16508015 ]
  25. Lai WS, Parker JS, Grissom SF, Stumpo DJ, Blackshear PJ: 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. doi: 10.1128/MCB.00945-06. Epub 2006 Oct 9. [PubMed:17030620 ]
  26. Franks TM, Lykke-Andersen J: TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 2007 Mar 15;21(6):719-35. doi: 10.1101/gad.1494707. [PubMed:17369404 ]
  27. Emmons J, Townley-Tilson WH, Deleault KM, Skinner SJ, Gross RH, Whitfield ML, Brooks SA: 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. doi: 10.1261/rna.748408. Epub 2008 Mar 26. [PubMed:18367721 ]
  28. Horner TJ, Lai WS, Stumpo DJ, Blackshear PJ: Stimulation of polo-like kinase 3 mRNA decay by tristetraprolin. Mol Cell Biol. 2009 Apr;29(8):1999-2010. doi: 10.1128/MCB.00982-08. Epub 2009 Feb 2. [PubMed:19188452 ]
  29. Hacker C, Valchanova R, Adams S, Munz B: ZFP36L1 is regulated by growth factors and cytokines in keratinocytes and influences their VEGF production. Growth Factors. 2010 Jun;28(3):178-90. doi: 10.3109/08977190903578660. [PubMed:20166898 ]
  30. Vignudelli T, Selmi T, Martello A, Parenti S, Grande A, Gemelli C, Zanocco-Marani T, Ferrari S: 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. doi: 10.1091/mbc.E10-01-0040. Epub 2010 Aug 11. [PubMed:20702587 ]
  31. Kedar VP, Darby MK, Williams JG, Blackshear PJ: Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85. PLoS One. 2010 Mar 8;5(3):e9588. doi: 10.1371/journal.pone.0009588. [PubMed:20221403 ]
  32. Chamboredon S, Ciais D, Desroches-Castan A, Savi P, Bono F, Feige JJ, Cherradi N: Hypoxia-inducible factor-1alpha mRNA: a new target for destabilization by tristetraprolin in endothelial cells. Mol Biol Cell. 2011 Sep;22(18):3366-78. doi: 10.1091/mbc.E10-07-0617. Epub 2011 Jul 20. [PubMed:21775632 ]
  33. Clement SL, Scheckel C, Stoecklin G, Lykke-Andersen J: Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol Cell Biol. 2011 Jan;31(2):256-66. doi: 10.1128/MCB.00717-10. Epub 2010 Nov 15. [PubMed:21078877 ]
  34. Holmes B, Artinian N, Anderson L, Martin J, Masri J, Cloninger C, Bernath A, Bashir T, Benavides-Serrato A, Gera J: Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress. Cell Signal. 2012 Jan;24(1):309-15. doi: 10.1016/j.cellsig.2011.09.015. Epub 2011 Sep 22. [PubMed:21964062 ]
  35. Adachi S, Homoto M, Tanaka R, Hioki Y, Murakami H, Suga H, Matsumoto M, Nakayama KI, Hatta T, Iemura S, Natsume T: ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK-RSK pathway. Nucleic Acids Res. 2014 Sep;42(15):10037-49. doi: 10.1093/nar/gku652. Epub 2014 Aug 8. [PubMed:25106868 ]
  36. Hausburg MA, Doles JD, Clement SL, Cadwallader AB, Hall MN, Blackshear PJ, Lykke-Andersen J, Olwin BB: Post-transcriptional regulation of satellite cell quiescence by TTP-mediated mRNA decay. Elife. 2015 Mar 27;4:e03390. doi: 10.7554/eLife.03390. [PubMed:25815583 ]
  37. Nowotarski SL, Origanti S, Sass-Kuhn S, Shantz LM: Destabilization of the ornithine decarboxylase mRNA transcript by the RNA-binding protein tristetraprolin. Amino Acids. 2016 Oct;48(10):2303-11. doi: 10.1007/s00726-016-2261-9. Epub 2016 May 19. [PubMed:27193233 ]
  38. Prenzler F, Fragasso A, Schmitt A, Munz B: Functional analysis of ZFP36 proteins in keratinocytes. Eur J Cell Biol. 2016 Aug;95(8):277-84. doi: 10.1016/j.ejcb.2016.04.007. Epub 2016 May 5. [PubMed:27182009 ]
  39. Huang L, Yu Z, Zhang Z, Ma W, Song S, Huang G: Interaction with Pyruvate Kinase M2 Destabilizes Tristetraprolin by Proteasome Degradation and Regulates Cell Proliferation in Breast Cancer. Sci Rep. 2016 Mar 1;6:22449. doi: 10.1038/srep22449. [PubMed:26926077 ]
  40. Peter D, Ruscica V, Bawankar P, Weber R, Helms S, Valkov E, Igreja C, Izaurralde E: Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression. Genes Dev. 2019 Oct 1;33(19-20):1355-1360. doi: 10.1101/gad.329219.119. Epub 2019 Aug 22. [PubMed:31439631 ]
  41. Fabian MR, Frank F, Rouya C, Siddiqui N, Lai WS, Karetnikov A, Blackshear PJ, Nagar B, Sonenberg N: Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin. Nat Struct Mol Biol. 2013 Jun;20(6):735-9. doi: 10.1038/nsmb.2572. Epub 2013 May 5. [PubMed:23644599 ]