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MAPKAP Kinase 2 Blocks Tristetraprolin-directed mRNA Decay by Inhibiting CAF1 Deadenylase Recruitment

Marchese, Francesco P., Aubareda, Anna, Tudor, Corina, Saklatvala, Jeremy, Clark, Andrew R., Dean, Jonathan L.E.·2010·Journal of Biological Chemistry
DOI 10.1074/jbc.m110.136473
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Crossref · 10.1074/jbc.m110.136473

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  • The CCR4-NOT deadenylase complex interacts with the C-terminus of ZFP36.

    “The CCR4-NOT deadenylase complex has recently been shown to interact with the C-terminus of ZFP36 (16,17); therefore, we next examined whether ZFP36L1 interacts with the CCR4-NOT deadenylase complex and whether this interaction is affected by PMA.”

    From ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK–RSK pathway (2014) · cites this paper as [16]

    The section on CAF1 recruitment (Fig. 9A–B; page unavailable) reports that CAF1a and CAF1b interact with TTP, supporting an association with a deadenylase complex. The experiments use full-length TTP and do not locate the interaction at its C-terminus; the paper describes the complex as CCR4–CAF1 rather than demonstrating an interaction with CCR4–NOT as a whole. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • The CCR4-NOT poly(A) deadenylase complex interacts with ZFP36 and ZFP36L1 and acts as an important effector complex of ZFP36-mediated mRNA-destabilization.

    “It is known to interact with ZFP36 and ZFP36L1 and to act as an important effector complex of ZFP36-mediated mRNA-destabilization (16,17).”

    From ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK–RSK pathway (2014) · cites this paper as [16]

    The Discussion (page unavailable) identifies CCR4–CAF1 as the main deadenylase complex involved in TTP-directed deadenylation, and the recruitment section reports that CAF1 interacts with TTP (ZFP36). Our copy does not establish an interaction with ZFP36L1, so that part of the attributed claim is unsupported. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • MAPKAPK2, a downstream kinase of p38, phosphorylates ZFP36, but not in the C-terminal region, leading to dissociation of ZFP36 and CNOT7.

    “Recently, MAPKAPK2, a downstream kinase of p38, has been shown to phosphorylate ZFP36, but not in the C-terminal region, leading to dissociation of ZFP36 and CNOT7 (16,17).”

    From ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK–RSK pathway (2014) · cites this paper as [16]

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Citations

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Research works printed but not linked: 43

  1. Dean, 1999, J. Biol. Chem., 274, 264, 10.1074/jbc.274.1.264 · DOI
  2. Winzen, 1999, EMBO J., 18, 4969, 10.1093/emboj/18.18.4969 · DOI
  3. Lasa, 2000, Mol. Cell. Biol., 20, 4265, 10.1128/MCB.20.12.4265-4274.2000 · DOI
  4. Mahtani, 2001, Mol. Cell. Biol., 21, 6461, 10.1128/MCB.21.9.6461-6469.2001 · DOI
  5. Chrestensen, 2004, J. Biol. Chem., 279, 10176, 10.1074/jbc.M310486200 · DOI
  6. Stoecklin, 2004, EMBO J., 23, 1313, 10.1038/sj.emboj.7600163 · DOI · Paper page
  7. Hitti, 2006, Mol. Cell. Biol., 26, 2399, 10.1128/MCB.26.6.2399-2407.2006 · DOI
  8. Tudor, 2009, FEBS Lett., 583, 1933, 10.1016/j.febslet.2009.04.039 · DOI
  9. Taylor, 1996, Immunity, 4, 445, 10.1016/S1074-7613(00)80411-2 · DOI
  10. Gherzi, 2004, Mol. Cell, 14, 571, 10.1016/j.molcel.2004.05.002 · DOI
  11. Winzen, 2007, Mol. Cell. Biol., 27, 8388, 10.1128/MCB.01493-07 · DOI
  12. Datta, 2008, J. Immunol., 180, 2545, 10.4049/jimmunol.180.4.2545 · DOI
  13. Tchen, 2004, J. Biol. Chem., 279, 32393, 10.1074/jbc.M402059200 · DOI
  14. Brook, 2006, Mol. Cell. Biol., 26, 2408, 10.1128/MCB.26.6.2408-2418.2006 · DOI
  15. Clark, 2009, Arthritis Rheum., 60, 3513, 10.1002/art.24919 · DOI
  16. Lai, 1999, Mol. Cell. Biol., 19, 4311, 10.1128/MCB.19.6.4311 · DOI
  17. Dean, 2003, J. Biol. Chem., 278, 39470, 10.1074/jbc.M306345200 · DOI
  18. Winzen, 2004, Mol. Cell. Biol., 24, 4835, 10.1128/MCB.24.11.4835-4847.2004 · DOI
  19. Johnson, 2002, J. Biol. Chem., 277, 18029, 10.1074/jbc.M110465200 · DOI
  20. Boeck, 1996, J. Biol. Chem., 271, 432, 10.1074/jbc.271.1.432 · DOI
  21. Tucker, 2001, Cell, 104, 377, 10.1016/S0092-8674(01)00225-2 · DOI
  22. Garneau, 2007, Nat. Rev. Mol. Cell Biol., 8, 113, 10.1038/nrm2104 · DOI · Paper page
  23. Lau, 2009, Biochem. J., 422, 443, 10.1042/BJ20090500 · DOI
  24. Yamashita, 2005, Nat. Struct. Mol. Biol., 12, 1054, 10.1038/nsmb1016 · DOI
  25. Zheng, 2008, J. Cell. Biol., 182, 89, 10.1083/jcb.200801196 · DOI
  26. Schwede, 2008, Nucleic Acids Res., 36, 3374, 10.1093/nar/gkn108 · DOI
  27. Lin, 2007, J. Biol. Chem., 282, 19958, 10.1074/jbc.M702281200 · DOI
  28. Lai, 2003, Mol. Cell. Biol., 23, 3798, 10.1128/MCB.23.11.3798-3812.2003 · DOI
  29. Chen, 2001, Cell, 107, 451, 10.1016/S0092-8674(01)00578-5 · DOI · Paper page
  30. Lykke-Andersen, 2005, Genes Dev., 19, 351, 10.1101/gad.1282305 · DOI
  31. Carballo, 2000, Blood, 95, 1891, 10.1182/blood.V95.6.1891 · DOI
  32. Brook, 2000, FEBS Lett., 483, 57, 10.1016/S0014-5793(00)02084-6 · DOI
  33. Tebo, 2003, J. Biol. Chem., 278, 12085, 10.1074/jbc.M212992200 · DOI
  34. Masters, 2001, J. Biol. Chem., 276, 45193, 10.1074/jbc.M105971200 · DOI
  35. Voeltz, 2001, Genes Dev., 15, 774, 10.1101/gad.872201 · DOI
  36. Dean, 2001, Mol. Cell. Biol., 21, 721, 10.1128/MCB.21.3.721-730.2001 · DOI
  37. Alford, 2007, J. Biol. Chem., 282, 6232, 10.1074/jbc.M610987200 · DOI
  38. Livak, 2001, Methods, 25, 402, 10.1006/meth.2001.1262 · DOI · Paper page
  39. Zekri, 2009, Mol. Cell. Biol., 29, 6220, 10.1128/MCB.01081-09 · DOI
  40. Rowlett, 2008, Am. J. Physiol. Gastrointest. Liver Physiol., 295, G421, 10.1152/ajpgi.00508.2007 · DOI
  41. Sun, 2007, J. Biol. Chem., 282, 3766, 10.1074/jbc.M607347200 · DOI
  42. Dehlin, 2000, EMBO J., 19, 1079, 10.1093/emboj/19.5.1079 · DOI
  43. Kedersha, 2005, J. Cell. Biol., 169, 871, 10.1083/jcb.200502088 · DOI

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Metadata

Authors
Marchese, F. P., Aubareda, A., Tudor, C., Saklatvala, J., Clark, A. R., & Dean, J. L. E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2010-09
Volume
285
Issue
36
Pages
27590-27600
ISSN
0021-9258
DOI
10.1074/jbc.m110.136473
Cited by
136
References
1
Language
en
Licence

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