The maximal size of protein to diffuse through the nuclear pore is larger than 60 kDa

FEBS Letters

Volumn 581, Issue 17, 2007, Pages 3164-3170

  Wang, Ruiwen ^a   Brattain, Michael G ^a  

^a ROSWELL PARK CANCER INSTITUTE   (United States)

Author keywords

Diffusion limit; Nuclear pore; Protein nuclear translocation

Indexed keywords

CHIMERIC PROTEIN; GREEN FLUORESCENT PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MYC PROTEIN;

ARTICLE; DIFFUSION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; MOLECULAR WEIGHT; NUCLEAR PORE; NUCLEAR PORE COMPLEX; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT;

ACTIVE TRANSPORT, CELL NUCLEUS; CELL NUCLEUS; DIFFUSION; GREEN FLUORESCENT PROTEINS; HCT116 CELLS; HELA CELLS; HUMANS; MITOGEN-ACTIVATED PROTEIN KINASE 1; MOLECULAR WEIGHT; NUCLEAR PORE; PARTICLE SIZE; PROTEINS; RECOMBINANT FUSION PROTEINS; TRANSFECTION; TUMOR CELLS, CULTURED;

EID: 34250807710     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.082     Document Type: Article

References (33)

1. Stoffler D., Fahrenkrog B., and Aebi U. The nuclear pore complex: from molecular architecture to functional dynamics. Curr. Opin. Cell Biol. 11 (1999) 391-401
2. Reichelt R., Holzenburg A., Buhle Jr. E.L., Jarnik M., Engel A., and Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110 (1990) 883-894
3. Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., and Matunis M.J. Proteomic analysis of the mammalian nuclear pore complex. J. Cell Biol. 158 (2002) 915-927
4. Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., and Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148 (2000) 635-651
5. Beck M., Forster F., Ecke M., Plitzko J.M., Melchior F., Gerisch G., Baumeister W., and Medalia O. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306 (2004) 1387-1390
6. Paine P.L. Nucleocytoplasmic movement of fluorescent tracers microinjected into living salivary gland cells. J. Cell Biol. 66 (1975) 652-657
7. Peters R. Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis. EMBO J. 3 (1984) 1831-1836
8. Feldherr C.M. The effect of the electron-opaque pore material on exchanges through the nuclear annuli. J. Cell Biol. 25 (1965) 43-53
9. Nigg E.A. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386 (1997) 779-787
10. Peters R. Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility. Biochim. Biophys. Acta 864 (1986) 305-359
11. Silver P.A. How proteins enter the nucleus. Cell 64 (1991) 489-497
12. Mattaj I.W., and Englmeier L. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67 (1998) 265-306
13. Gorlich D. Transport into and out of the cell nucleus. EMBO J. 17 (1998) 2721-2727
14. Weis K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112 (2003) 441-451
15. Gorlich D., and Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15 (1999) 607-660
16. Faleiro L., and Lazebnik Y. Caspases disrupt the nuclear-cytoplasmic barrier. J. Cell Biol. 151 (2000) 951-959
17. Harootunian A.T., Adams S.R., Wen W., Meinkoth J.L., Taylor S.S., and Tsien R.Y. Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion. Mol. Biol. Cell 4 (1993) 993-1002
18. Wen W., Meinkoth J.L., Tsien R.Y., and Taylor S.S. Identification of a signal for rapid export of proteins from the nucleus. Cell 82 (1995) 463-473
19. Widmann C., Gibson S., Jarpe M.B., and Johnson G.L. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79 (1999) 143-180
20. Bogoyevitch M.A., and Court N.W. Counting on mitogen-activated protein kinases - ERKs 3, 4, 5, 6, 7 and 8. Cell. Signal. 16 (2004) 1345-1354
21. Whitehurst A.W., Wilsbacher J.L., You Y., Luby-Phelps K., Moore M.S., and Cobb M.H. ERK2 enters the nucleus by a carrier-independent mechanism. Proc. Natl. Acad. Sci. USA 99 (2002) 7496-7501
22. Matsubayashi Y., Fukuda M., and Nishida E. Evidence for existence of a nuclear pore complex-mediated, cytosol-independent pathway of nuclear translocation of ERK MAP kinase in permeabilized cells. J. Biol. Chem. 276 (2001) 41755-41760
23. Alessi D.R., et al. 3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. Curr. Biol. 7 (1997) 776-789
24. Mora A., Komander D., van Aalten D.M., and Alessi D.R. PDK1, the master regulator of AGC kinase signal transduction. Semin. Cell Dev. Biol. 15 (2004) 161-170
25. Lim M.A., Kikani C.K., Wick M.J., and Dong L.Q. Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function. Proc. Natl. Acad. Sci. USA 100 (2003) 14006-14011
26. Bonner W.M. Protein migration and accumulation in nuclei. In: Busch H. (Ed). The Cell Nucleus (1978), Academic Press, New York 97-148
27. Feldherr C.M., and Marshall Jr. J.M. The use of colloidal gold for studies of intracellular exchanges in the ameba Chaos chaos. J. Cell Biol. 12 (1962) 640-645
28. Feldherr C.M. The nuclear annuli as pathways for nucleocytoplasmic exchanges. J. Cell Biol. 14 (1962) 65-72
29. Horowitz S.B., and Moore L.C. The nuclear permeability, intracellular distribution, and diffusion of inulin in the amphibian oocyte. J. Cell Biol. 60 (1974) 405-415
30. Paine P.L., and Feldherr C.M. Nucleocytoplasmic exchange of macromolecules. Exp. Cell Res. 74 (1972) 81-98
31. Bonner W.M. Protein migration into nuclei. I. Frog oocyte nuclei in vivo accumulate microinjected histones, allow entry to small proteins, and exclude large proteins. J. Cell Biol. 64 (1975) 421-430
32. Stacey D.W., and Allfrey V.G. Microinjection studies of protein transit across the nuclear envelope of human cells. Exp. Cell Res. 154 (1984) 283-292
33. Stoffler D., Schwarz-Herion K., Aebi U., and Fahrenkrog B. Getting across the nuclear pore complex: new insights into nucleocytoplasmic transport. Can. J. Physiol. Pharmacol. 84 (2006) 499-507