Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

doi:10.1083/jcb.111.3.807

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Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

SA Adam, RS Marr and L Gerace
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.

We have developed an in vitro system involving digitonin-permeabilized vertebrate cells to study biochemical events in the transport of macromolecules across the nuclear envelope. While treatment of cultured cells with digitonin permeabilizes the plasma membranes to macromolecules, the nuclear envelopes remain structurally intact and nuclei retain the ability to transport and accumulate proteins containing the SV40 large T antigen nuclear location sequence. Transport requires addition of exogenous cytosol to permeabilized cells, indicating the soluble cytoplasmic factor(s) required for nuclear import are released during digitonin treatment. In this reconstituted import system, a protein containing a nuclear location signal is rapidly accumulated in nuclei, where it reaches a 30-fold concentration compared to the surrounding medium within 30 min. Nuclear import is specific for a functional nuclear location sequence, requires ATP and cytosol, and is temperature dependent. Furthermore, accumulation of the transport substrate within nuclei is completely inhibited by wheat germ agglutinin, which binds to nuclear pore complexes and inhibits transport in vivo. Together, these results indicate that the permeabilized cell system reproduces authentic nuclear protein import. In a preliminary biochemical dissection of the system, we observe that the sulfhydryl alkylating reagent N- ethylmaleimide inactivates both cytosolic factor(s) and also component(s) in the insoluble permeabilized cell fraction required for nuclear protein import. Because this permeabilized cell model is simple, efficient, and works effectively with cells and cytosol fractions prepared from a variety of different vertebrate sources, it will prove powerful for investigating the biochemical pathway of nuclear transport.
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Le Rouzic, E., Mousnier, A., Rustum, C., Stutz, F., Hallberg, E., Dargemont, C., Benichou, S. (2002). Docking of HIV-1 Vpr to the Nuclear Envelope Is Mediated by the Interaction with the Nucleoporin hCG1. J. Biol. Chem. 277: 45091-45098 [Abstract] [Full Text]
Apostolova, M. D., Ivanova, I. A., Dagnino, C., D'Souza, S. J. A., Dagnino, L. (2002). Active Nuclear Import and Export Pathways Regulate E2F-5 Subcellular Localization. J. Biol. Chem. 277: 34471-34479 [Abstract] [Full Text]
Bauerle, M., Doenecke, D., Albig, W. (2002). The Requirement of H1 Histones for a Heterodimeric Nuclear Import Receptor. J. Biol. Chem. 277: 32480-32489 [Abstract] [Full Text]
Prufer, K., Barsony, J. (2002). Retinoid X Receptor Dominates the Nuclear Import and Export of the Unliganded Vitamin D Receptor. Mol. Endocrinol. 16: 1738-1751 [Abstract] [Full Text]
Gustin, K. E., Sarnow, P. (2002). Inhibition of Nuclear Import and Alteration of Nuclear Pore Complex Composition by Rhinovirus. J. Virol. 76: 8787-8796 [Abstract] [Full Text]
Hang, J., Dasso, M. (2002). Association of the Human SUMO-1 Protease SENP2 with the Nuclear Pore. J. Biol. Chem. 277: 19961-19966 [Abstract] [Full Text]
Thompson, K. J., Fried, M. G., Ye, Z., Boyer, P., Connor, J. R. (2002). Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei. J. Cell Sci. 115: 2165-2177 [Abstract] [Full Text]