A part of the transmembrane domain of pro-TNF can function as a cleavable signal sequence that generates a biologically active secretory form of TNF

Journal of Biochemistry

Volumn 126, Issue 2, 1999, Pages 413-420

  Ishisaka, Rumi ^a   Sato, Noriyuki ^a   Tanaka, Kenji ^a   Takeshige, Tomonori ^a   Iwata, Hiroyuki ^a   Klostergaard, Jim ^b   Utsumi, Toshihiko ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

^b UNIVERSITY OF TEXAS   (United States)

Author keywords

Membrane translocation; Processing; Secretion; Signal sequence; Tumor necrosis factor

Indexed keywords

MUTANT PROTEIN; PROTEIN PRECURSOR; TUMOR NECROSIS FACTOR;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DOG; ENDOPLASMIC RETICULUM; GENETIC TRANSFECTION; HYDROPHOBICITY; MEMBRANE TRANSPORT; MICROSOME MEMBRANE; MOLECULAR WEIGHT; NONHUMAN; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS;

ANIMALIA; CANIS FAMILIARIS;

EID: 0032818715     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022466     Document Type: Article

References (32)

1. Vilcek, J. and Lee, T.H. (1991) Tumor necrosis factor. New insights into the molecular mechanisms of its multiple actions. J. Biol. Chem. 266, 7313-7316
2. Kriegler, M., Perez, C., DeFay, K., Albert, I., and Lu, S.D. (1988) A novel form of TNF/Cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF. Cell 53, 45-53
3. Tang, P., Hung, M-C., and Klostergaard, J. (1996) Human pro-tumor necrosis factor is a homotrimer. Biochemistry 35, 8216-8225
4. Perez, C., Albert, I., DeFay, K., Zachariades, N., Gooding, L., and Kriegler, M. (1990) A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact. Cell 63, 251-258
5. Grell, M., Douni, E., Wajant, H., Löhden, M., Clauss, M., Maxeiner, B., Georgopoulos, S., Lesslauer, W., Kollias, G., Pfizenmaier, K., and Scheurich, P. (1995) The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 83, 793-802
6. + T cells is mediated by macrophages through interaction of HIV gp 120 with chemokine receptor CXCR4. Nature 395, 189-194
7. Black, R.A., Rauch, C.T., Kozlosky, C.J., Peschon, J.J., Slack, J.L., Wolson, M.F., Castner, B.J., Stocking, K.L., Reddy, P., Srinivasan, S., Nelson, N., Boiani, N., Schooley, K.A., Gerhart, M., Davis, R., Fitzner, J.N., Johnson, R.S., Paxton, R.J., March, C.J., and Cerretti, D.P. (1997) A metalloproteinase disintegrin that releases tumor necrosis factor-α from cells. Nature 385, 729-733
8. Moss, M.L., Jin, S.-L.C., Milla, M.E., Burkhart, W., Carter, H.L., Chen, W.J., Clay, W.C., Didsburry, J.R., Hassler, D., Hoffman, C.R., Kost, T.A., Lambert, M.H., Leesnitzer, M.A., McCauley, P., McGeehan, G., Mitchell, J., Moyer, M., Pahel, G., Rocque, W., Overton, L.K., Schoenen, F., Seaton, T., Su, J.-L., Warner, J., Willard, D., and Becherer, J.D. (1997) Cloning of a disintegrin metalloproteinase that processes precursor tumor-necrosis factor-α. Nature 385, 733-736
9. Utsumi, T., Levitan, A., Hung, M-C., and Klostergaard, J. (1993) Effect of truncation of human pro-tumor necrosis factor transmembrane domain on cellular targeting. J. Biol. Chem. 268, 9511-9516
10. Utsumi, T., Akimaru, K., Kawabata, Z., Levitan, A., Tokunaga, T., Tang, P., Ide, A., Hung, M-C., and Klostergaard, J. (1995) Human pro-tumor necrosis factor: Molecular determinants of membrane translocation, sorting, and maturation. Mol. Cell. Biol. 15, 6398-6405
11. Utsumi, T., Kuranami, J., Tou, E., Ide, A., Akimaru, K., Hung, M-C., and Klostergaard, J. (1996) In vitro synthesis of an N-myristoylated fusion protein that binds to the liposomal surface. Arch. Biochem. Biophys. 326, 179-184
12. Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467
13. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 22, 680-685
14. Utsumi, T., Klostergaard, J., Akimaru, K., Edashige, K., Sato, E.F., and Utsumi, K. (1992) Modulation of TNF-α-priming and stimulation-dependent superoxide generation in human neutrophils by protein kinase inhibitors. Arch. Biochem. Biophys. 294, 271-278
15. von Heijne, G. (1985) Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105
16. von Heijne, G. (1990) The signal peptide. J. Membr. Biol. 115, 195-201
17. Bieker, K.L., Phillips, G.J., and Silhavy, T. J. (1990) The sec and prl genes of Escherichia coli. J. Bioenerg. Biomembr. 22, 291-310
18. Rapoport, T.A. (1992) Transport of protein across the endoplasmic reticulum membrane. Science 258, 931-936
19. Gennity, J., Goldstein, J., and Inouye, M. (1990) Signal peptide mutants of Escherichia coli. J. Bioenerg. Biomembr. 22, 233-269
20. Bird, P., Gething, M.-J., and Sambrook, J. (1990) The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity. J. Biol. Chem. 265, 8420-8425
21. Jungnickel, B. and Rapoport, T.A. (1995) A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270
22. Belin, D., Bost, S., Vassalli, J.-D., and Strub, K. (1996) A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15, 468-478
23. Hatsuzawa, K., Tagaya, M., and Mizushima, S. (1997) The hydrophobic region of signal peptide is a determinant for SRP recognition and protein translocation across the ER membrane. J. Biochem. 121, 270-277
24. Sato, T., Sakaguchi, M., Mihara, K., and Omura, T. (1990) The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane. EMBO J. 9, 2391-2397
25. Sakaguchi, M., Tomiyoshi, R., Kuroiwa, T., Mihara, K., and Omura, T. (1992) Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge. Proc. Natl. Acad. Sci. USA 89, 16-19
26. Nilsson, I., Whitley, P., and von Heijne, G. (1994) The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol. 126, 1127-1132
27. Paetzel, M., Dalbey, R.E., and Strynadka, N.C.J. (1998) Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature 396, 186-190
28. Wingfield, P., Pain, R.H., and Craig, S. (1987) Tumor necrosis factor is a compact trimer. FEBS Lett. 221, 179-184
29. Jones, E.Y., Stuart, D.I., and Walker, N.P.C. (1989) Structure of tumor necrosis factor. Nature 338, 225-228
30. Eck, M.J., Ultsch, M., Rinderknecht, E., de Vos, A.M., and Sprang, S.R. (1992) The structure of human lymphotoxin (tumor necrosis factor-β) at 1.9-Å resolution. J. Biol. Chem. 267, 2119-2122
31. Gething, M.J., McCammon, K., and Sambrook, J. (1986) Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport. Cell 46, 939-950
32. Braakman, I., Hoover-Litty, H., Wagner, K.R., and Helenius, A. (1991) Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114, 401-411