Nuclear calcium and the regulation of the nuclear pore complex

BioEssays

Volumn 19, Issue 9, 1997, Pages 787-792

  Perez Terzic, Carmen ^a   Jaconi, Marisa ^a   Clapham, David E ^a,b  

^a MAYO CLINIC   (United States)

^b BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; EUKARYOTA;

EID: 0031239585     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190908     Document Type: Review

References (69)

1. Csermely, C., Schnaider, T. and Szanto, I. (1995). Signalling and transport through the nuclear membrane. Biochem. Biophys. Acta 1241, 425-452.
2. Pante, N. and Aebi, U. (1993). The nuclear pore complex. J. Cell Biol. 122, 977-984.
3. Jelsema, C. L. and Morre, D. J. (1978). Distribution of phospholipid biosynthetic enzymes among cell components of rat liver. J. Biol. Chem. 253, 7960-7971.
4. Fahl, W. E., Jefcoate, C. R. and Kasper, C. B. (1978). Characteristics of benzo(a)pyrene metabolism and cytochrome P-450 heterogeneity in rat liver nuclear envelope and comparison to microsomal membrane. J. Biol. Chem. 253, 3106-3113.
5. Moir, R. D. and Goldman, R. D. (1993). Lamin dynamics. Curr. Opin. Cell Biol. 5, 408-411.
6. Gerace, L. and Burke, B. (1988). Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4, 335-374.
7. Fabre, E. and Hurt, E. C. (1994). Nuclear transport. Curr. Opin. Cell Biol. 6, 335-342.
8. Snow, C. M., Senior, A. and Gerace, L. (1987). Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell. Biol. 104, 1143-1156.
9. Finlay, D. R. and Forbes, D. J. (1990). Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60, 17-29.
10. Rout, M. P. and S.R., W. (1994). Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4, 357-365.
11. Franke, W. W. (1974). Structure, biochemistry and functions of the nuclear envelope. Int. Rev. Cytol. Suppl. 4, 71-236.
12. Akey, C. W. (1995). Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248, 273-293.
13. Akey, C. W. (1989). Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J. Cell Biol. 109, 955-970.
14. Hinshaw, J. E., Carragher, B. O. and Milligan, R. A. (1992). Architecture and design of the nuclear pore complex. Cell 69, 1133-1141.
15. Akey, C. W. (1993). Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1-19.
16. Hanover, J. A. (1992). The nuclear pore: at the crossroads. FASEB J. 6, 2288-2295.
17. Jarnik, M. and Aeibi, U. (1991). Towards a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol. 107, 291-308.
18. Goldberg, M. W. and Allen, T. D. (1992). High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol. 119, 1429-1440.
19. Goldberg, M. W. and Allen, T. D. (1995). Structural and functional organization of the nuclear envelope. Curr Opin. Cell Biol. 7, 301-309.
20. Pante, N and Aebi, U. (1996). Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Science 273, 1729-1732.
21. Hicks, G. R. and Raikhel, N. V. (1995). Protein import into the nucleus: an integrate view. Annu. Rev. Cell. Dev. Biol. 11, 155-188.
22. Gorlich, D. and Mattaj, I. W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
23. Dingwall, C., Sharnick, S. V. and Laskey, R. A. (1982). A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30, 449-458.
24. Nehrbass, U. and Blobel, G. (1996). Role of the nuclear transport factor p10 in nuclear import. Science 272, 120-122.
25. Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W. and Luhrmann, R. (1995). The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483.
26. Newmeyer, D. and Forbes, D. J. (1988). Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell 52, 641-653.
27. Bonner, W. M. (1975). Protein migration into nuclei. I. Frog oocyte nuclei accumulate a class of microinjected oocyte nuclear proteins and exclude a class of microinjected oocyte cytoplasmic proteins. J. Cell Biol. 64, 431-437.
28. Sullivan, K. M. C. and Wilson, K. L. (1994). A new role for IP3 receptors: Calcium release during nuclear vesicle fusion. Cell Calcium 16, 314-321.
29. Roche, E. and Prentki, M. (1994). Calcium regulation of immediate-early response genes. Cell Calcium 16, 331-338.
30. Srinivasan, M., Edman, C. F. and Schulman, H. (1994). Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus. J. Cell Biol. 126, 839-852.
31. Bachs, O., Agell, N. and Carafoli, E. (1992). Calcium and calmodulin fucntion in the cell nucleus. Biochem. Biophys. Acta 1113, 259-270.
32. Bachs, O., Agell, N. and Carafoli, E. (1994). Calmodulin and calmodulin-binding proteins in the nucleus. Cell Calcium 16, 289-296.
33. Hernandez-Cruz, A., Sala, F. and Adams, P. R. (1990). Subcellular calcium transients visualized by confocal microscopy in a voltage-clamped vertebrate neuron. Science 247, 858-862.
34. Waybill, M. M. et al. (1991). Nuclear calcium gradients in cultured rat hepatocytes. Am. J. Physiol. 261, E49-E57.
35. Al-Mohanna, F. A., Caddy, K. W. T. and Bolsover, S. R. (1994). The nucleus is isolated from large cytosolic calcium ion changes. Nature 367, 745-750.
36. Brini, M., Marsault, R., Bastianutto, C., Pozzan, T. and Rizzuto, R. (1994). Nuclear targeting of aequorin: A new approach for measuring nuclear calcium concentration in intact cells. Cell Calcium, 16, 259-268.
37. Allbritton, N.L., Oancea, E., Kuhn, M.A. and Meyer, T. (1994). Source of nuclear Calcium signals. Proc. Natl Acad. Sci. USA 91, 12458-12462.
38. Lanini, L., Bachs, O. and Carafoli, E. (1992). The calcium pump of the liver nuclear membrane is identical to that of endoplasmic reticulum. J. Biol. Chem. 267, 11548-1552.
39. 2+ from the nuclear envelope. Cell 80, 439-444.
40. Nicotera, P., Orrenius, S., Nilsson, T. and Berggren, P. O. (1990). An inositol 1,4,5-trisphosphate-sensitive calcium pool in liver nuclei. Proc. Natl Acad. Sci. USA 87, 6868-6862.
41. Stehno-Bittel, L., Luckhoff, A. and Clapham, D. E. (1995). Calcium release from the nucleus by InsP3 receptor channels. Neuron 14, 163-167.
42. Mak, D. O. and Foskett, J. K. (1994). Single-channel inositol 1,4,5-trisphosphate receptor currents revealed by patch clamp of isolated Xenopus oocyte nuclei. J. Biol. Chem. 269, 29375-29378.
43. 2+ concentration. J. Biol. Chem. 270, 4959-4962.
44. 2+ signaling by inositol 1,4,5-trisphosphate. Discrete distribution of inositol phosphates receptors to inner and outer nuclear membranes. J. Biol. Chem. 271, 478-485.
45. Cocco, L., Martelli, A. M. and Gilmour, R. S. (1994). Inositol lipid cycle in the nucleus. Cellular Signalling 6, 481-485.
46. Matter, N., Ritz, M. F., Freyermuth, S., Rogue, P. and A.N., M. (1993). Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei. J. Biol. Chem. 268, 732-736.
47. Malviya, A. N. (1994). The nuclear inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate receptors. Cell Calcium 16, 301-313.
48. Koppler, P., Mersel, M., Humbert, J. P., Vignon, J., Vincendon, G. and Malviya, A. N. (1996). High affinity inositol 1,3,4,5-tetrakisphosphate receptor from rat liver nuclei: purification, characterization, and amino-terminal sequence. Biochemistry 35, 5481-5487.
49. Stehno-Bittel, L., Perez-Terzic, C., Luckhoff, A. and Clapham, D. E. (1996). Nuclear ion channels and regulation of the nuclear pore. In Organellar Ion Channels and Transporters. Society of General Physiologists, Vol. 51 (ed. D. E. Clapham and B. E. Ehrlich), pp.195-207. RUP, New York.
50. Greber, U. F. and Gerace, L. (1992). Nuclear import protein is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein. J. Cell. Biol. 116, 15-30.
51. Featherstone, C., Darby, M. K. and Gerace, L. (1988). A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of proteins and RNA in vivo. J. Cell Biol. 107, 1289-1297.
52. Greber, U. F. and Gerace, L. (1995). Depletion of calcium from the lumen of endoplasmic reticulum reversible inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell. Biol. 128, 5-14.
53. Stehno-Bittel, L., Perez-Terzic, C. and Clapham, D. E. (1995). Diffusion across the nuclear envelope inhibited by depletion of the nuclear calcium store. Science 270, 1835-1838.
54. Folprecht, G., Schneider, S., and Oberleithner, H. (1996). Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy. Eur. J. Physiol. 432, 831-838.
55. Akey, C. W. and Goldfarb, D. S. (1989). Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109, 971-982.
56. Akey, C. W. (1990). Visualization of transport-related configurations of the nuclear pore transporter. Biophys. J. 58, 341-355.
57. Hinshaw, J. E. (1994). Architecture of the nuclear pore complex and its involvement in nucleocytoplasmic transport. Biochem. Pharm. 47, 15-20.
58. 2+ stores. Science 273, 1875-1877.
59. Greber, U. F., Senior, A. and Gerace, L. (1990). A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 9, 1495-1502.
60. Wozniak, R. W. and Blobel, G. (1992). The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J. Cell Biol. 119, 1441-1449.
61. Pines, J. and Hunter, T. (1991). Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J. Cell Biol. 115, 1-17.
62. Inagaki, N., Ito, M., Nakano, T. and Inagaki, M. (1994). Spatiotemporal distribution of protein kinase and phosphatase activities. Trends Biochem. Sci. 19, 448-452.
63. Feldherr, C. M. and Akin, D. (1990). The permeability of the nuclear envelope in dividing and non dividing cell cultures. J. Cell Biol. 111, 1-8.
64. York, J. D. and Majerus, P. W. (1994). Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells. J. Biol. Chem. 269, 7847-7850.
65. Jiang, L. W. and Schindler, M. (1988). Nuclear transport in 3T3 fibroblasts: effects of growth factors, transformation, and cell shape. J. Cell Biol. 106, 13-19.
66. Deisseroth, K., Bito, H. and Tsien, R.W. (1997). Signaling from synapse to nucleus: postsynaptic CREB phosphorylation during multiple forms of hippocampal synaptic plasticity. Neuron 16, 89-101.
67. Hardingham, G.E., Chawla S., Johnson, C.M. and Bading, H. (1997). Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression. Nature 385, 260-265.
68. Nigg, E.A. (1990). Mechanism of the signal transduction to the cell nucleus. Adv. Cancer. Res. 55, 271-310.
69. Nigg, E.A. (1997). Nucleocytoplasmic transport: signals, mechanism and regulation. Nature 386, 779-787.