Lysine fatty acylation promotes lysosomal targeting of TNF-α

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Jiang, Hong ^a,b   Zhang, Xiaoyu ^a   Lin, Hening ^a  

^a Department of Obstetrics Gynecology   (United States)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; TUMOR NECROSIS FACTOR;

ACYLATION; CELL LINE; CELL ORGANELLE; CYTOPLASM VESICLE; HUMAN; LYSOSOME; METABOLISM; PROTEIN DEGRADATION; PROTEIN TRANSPORT;

ACYLATION; CELL LINE; CYTOPLASMIC VESICLES; HUMANS; LYSINE; LYSOSOMES; ORGANELLES; PROTEIN TRANSPORT; PROTEOLYSIS; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84964409712     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep24371     Document Type: Article

References (34)

1. Locksley, R. M., Killeen, N., Lenardo, M. J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487-501 (2001).
2. Croft, M. The role of TNF superfamily members in T-cell function and diseases. Nature reviews. Immunology 9, 271-285, doi: 10.1038/nri2526 (2009).
3. Caminero, A., Comabella, M., Montalban, X. Tumor necrosis factor alpha (TNF-alpha), anti-TNF-alpha and demyelination revisited: an ongoing story. Journal of neuroimmunology 234, 1-6, doi: 10.1016/j.jneuroim.2011.03.004 (2011).
4. Wajant, H., Pfizenmaier, K., Scheurich, P. Tumor necrosis factor signaling. Cell death and differentiation 10, 45-65, doi: 10.1038/sj.cdd.4401189 (2003).
5. Gaur, U., Aggarwal, B. B. Regulation of proliferation, survival and apoptosis by members of the TNF superfamily. Biochemical pharmacology 66, 1403-1408 (2003).
6. Aggarwal, B. B., Gupta, S. C., Kim, J. H. Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey. Blood 119, 651-665, doi: 10.1182/blood-2011-04-325225 (2012).
7. Palladino, M. A., Bahjat, F. R., Theodorakis, E. A., Moldawer, L. L. Anti-TNF-alpha therapies: the next generation. Nature reviews. Drug discovery 2, 736-746, doi: 10.1038/nrd1175 (2003).
8. Horiuchi, T., Mitoma, H., Harashima, S., Tsukamoto, H., Shimoda, T. Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents. Rheumatology 49, 1215-1228, doi: 10.1093/rheumatology/keq031 (2010).
9. Murray, R. Z., Kay, J. G., Sangermani, D. G., Stow, J. L. A Role for the Phagosome in Cytokine Secretion. Science 310, 1492-1495, doi: 10.1126/science.1120225 (2005).
10. Stanley, A. C., Lacy, P. Pathways for cytokine secretion. Physiology 25, 218-229, doi: 10.1152/physiol.00017.2010 (2010).
11. Duitman, E. H., Orinska, Z., Bulfone-Paus, S. Mechanisms of cytokine secretion: a portfolio of distinct pathways allows flexibility in cytokine activity. European journal of cell biology 90, 476-483, doi: 10.1016/j.ejcb.2011.01.010 (2011).
12. Stow, J. L., Low, P. C., Offenhauser, C., Sangermani, D. Cytokine secretion in macrophages and other cells: pathways and mediators. Immunobiology 214, 601-612, doi: 10.1016/j.imbio.2008.11.005 (2009).
13. Black, R. A. et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385, 729-733, doi: 10.1038/385729a0 (1997).
14. Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385, 733-736, doi: 10.1038/385733a0 (1997).
15. Eck, M. J., Sprang, S. R. The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. The Journal of biological chemistry 264, 17595-17605 (1989).
16. Jones, E. Y., Stuart, D. I., Walker, N. P. Structure of tumour necrosis factor. Nature 338, 225-228, doi: 10.1038/338225a0 (1989).
17. Smith, R. A., Baglioni, C. The active form of tumor necrosis factor is a trimer. The Journal of biological chemistry 262, 6951-6954 (1987).
18. Tang, P., Hung, M. C., Klostergaard, J. Human pro-tumor necrosis factor is a homotrimer. Biochemistry 35, 8216-8225, doi: 10.1021/bi952182t (1996).
19. Wingfield, P., Pain, R. H., Craig, S. Tumour necrosis factor is a compact trimer. FEBS letters 211, 179-184 (1987).
20. Friedmann, E. et al. SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production. Nature cell biology 8, 843-848, doi: 10.1038/ncb1440 (2006).
21. Fluhrer, R. et al. A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b. Nature cell biology 8, 894-896, doi: 10.1038/ncb1450 (2006).
22. Takakura-Yamamoto, R., Yamamoto, S., Fukuda, S., Kurimoto, M. O-glycosylated species of natural human tumor-necrosis factoralpha. European journal of biochemistry 235, 431-437 (1996).
23. Sherry, B., Jue, D. M., Zentella, A., Cerami, A. Characterization of high molecular weight glycosylated forms of murine tumor necrosis factor. Biochemical and biophysical research communications 173, 1072-1078 (1990).
24. Olszewski, M. B., Trzaska, D., Knol, E. F., Adamczewska, V., Dastych, J. Efficient sorting of TNF-alpha to rodent mast cell granules is dependent on N-linked glycosylation. European journal of immunology 36, 997-1008, doi: 10.1002/eji.200535323 (2006).
25. Utsumi, T. et al. Transmembrane TNF (pro-TNF) is palmitoylated. FEBS letters 500, 1-6 (2001).
26. Poggi, M. et al. Palmitoylation of TNF alpha is involved in the regulation of TNF receptor 1 signalling. Biochimica et biophysica acta 1833, 602-612, doi: 10.1016/j.bbamcr.2012.11.009 (2013).
27. Stevenson, F. T., Bursten, S. L., Locksley, R. M., Lovett, D. H. Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues. The Journal of experimental medicine 176, 1053-1062 (1992).
28. Jiang, H. et al. SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine. Nature 496, 110-113, doi: 10.1038/nature12038 (2013).
29. rews, N. W. Regulated secretion of conventional lysosomes. Trends in cell biology 10, 316-321 (2000).
30. Hashida, S., Towatari, T., Kominami, E., Katunuma, N. Inhibitions by E-64 derivatives of rat liver cathepsin B and cathepsin L in vitro and in vivo. Journal of biochemistry 88, 1805-1811 (1980).
31. Stevenson, F. T., Bursten, S. L., Fanton, C., Locksley, R. M., Lovett, D. H. The 31-kDa precursor of interleukin 1 alpha is myristoylated on specific lysines within the 16-kDa N-terminal propiece. Proceedings of the National Academy of Sciences of the United States of America 90, 7245-7249 (1993).
32. Lahat, N. et al. Hypoxia enhances lysosomal TNF-alpha degradation in mouse peritoneal macrophages. American journal of physiology. Cell physiology 295, C2-12, doi: 10.1152/ajpcell.00572.2007 (2008).
33. Lim, J. H. et al. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Molecular cell 38, 864-878, doi: 10.1016/j.molcel.2010.05.023 (2010).
34. Li, Q. et al. A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J. Neurosci. 24, 4070-4081 (2004).