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Science 25 October 1996: Vol. 274. no. 5287, pp. 624 - 627 DOI: 10.1126/science.274.5287.624
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Reports
Kap104p: A Karyopherin Involved in the Nuclear Transport of
Messenger RNA Binding Proteins
John D. Aitchison,
Günter Blobel,
*
Michael P. Rout
A cytosolic yeast karyopherin, Kap104p, was isolated and shown to
function in the nuclear import of a specific class of proteins. The
protein bound directly to repeat-containing nucleoporins and to a
cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins,
Nab2p and Nab4p. Depletion of Kap104p resulted in a rapid shift of
Nab2p from the nucleus to the cytoplasm without affecting the
localization of other nuclear proteins tested. This finding suggests
that the major function of Kap104p lies in returning mRNA binding
proteins to the nucleus after mRNA export.
Laboratory of Cell Biology, Howard Hughes Medical Institute,
Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
*
To whom correspondence should be addressed. E-mail:
blobel{at}rockvax.rockefeller.edu
Read the Full Text
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- Yeast Los1p Has Properties of an Exportin-Like Nucleocytoplasmic Transport Factor for tRNA.
- K. Hellmuth, D. M. Lau, F. R. Bischoff, M. Künzler, E. Hurt, and G. Simos (1998)
Mol. Cell. Biol.
18, 6374-6386
| Abstract »
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- Cse1p Is Involved in Export of Yeast Importin alpha from the Nucleus.
- J. Solsbacher, P. Maurer, F. R. Bischoff, and G. Schlenstedt (1998)
Mol. Cell. Biol.
18, 6805-6815
| Abstract »
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- Ran and Nuclear Transport.
- M. S. Moore (1998)
J. Biol. Chem.
273, 22857-22860
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- Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121.
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Genes & Dev.
12, 2673-2683
| Abstract »
| Full Text »
- Interaction of the Human Immunodeficiency Virus Type 1 Vpr Protein with the Nuclear Pore Complex.
- R. A. M. Fouchier, B. E. Meyer, J. H. M. Simon, U. Fischer, A. V. Albright, F. Gonzalez-Scarano, and M. H. Malim (1998)
J. Virol.
72, 6004-6013
| Abstract »
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- Functional Conservation of the Transportin Nuclear Import Pathway in Divergent Organisms.
- M. C. Siomi, M. Fromont, J.-C. Rain, L. Wan, F. Wang, P. Legrain, and G. Dreyfuss (1998)
Mol. Cell. Biol.
18, 4141-4148
| Abstract »
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- A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.
- T. Taura, H. Krebber, and P. A. Silver (1998)
PNAS
95, 7427-7432
| Abstract »
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- The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export.
- J. L. Watkins, R. Murphy, J. L. T. Emtage, and S. R. Wente (1998)
PNAS
95, 6779-6784
| Abstract »
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- Identification and Functional Characterization of a Novel Nuclear Localization Signal Present in the Yeast Nab2 Poly(A)+ RNA Binding Protein.
- R. Truant, R. A. Fridell, R. E. Benson, H. Bogerd, and B. R. Cullen (1998)
Mol. Cell. Biol.
18, 1449-1458
| Abstract »
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- HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection.
- M. A. Vodicka, D. M. Koepp, P. A. Silver, and M. Emerman (1998)
Genes & Dev.
12, 175-185
| Abstract »
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- Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export.
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J. Cell Sci.
111, 223-236
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- A Distinct and Parallel Pathway for the Nuclear Import of an mRNA-binding Protein.
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J. Cell Biol.
139, 1645-1653
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- A Nuclear Import Pathway for a Protein Involved in tRNA Maturation.
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J. Cell Biol.
139, 1655-1661
| Abstract »
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- Evolutionary specialization of the nuclear targeting apparatus.
- H. S. Malik, T. H. Eickbush, and D. S. Goldfarb (1997)
PNAS
94, 13738-13742
| Abstract »
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- Ran-unassisted Nuclear Migration of a 97-kD Component of Nuclear Pore-targeting Complex.
- S. Kose, N. Imamoto, T. Tachibana, T. Shimamoto, and Y. Yoneda (1997)
J. Cell Biol.
139, 841-849
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