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Science 19 May 1995:
Vol. 268. no. 5213, pp. 1049 - 1053
DOI: 10.1126/science.7754385

Articles

Science, Vol 268, Issue 5213, 1049-1053
Copyright © 1995 by American Association for the Advancement of Science


articles

Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences

K Weis, IW Mattaj, and AI Lamond

European Molecular Biology Laboratory, Heidelberg, Germany.

Import of proteins into the nucleus is a two-step process, involving nuclear localization sequence (NLS)-dependent docking of the substrate at the nuclear envelope followed by translocation through the nuclear pore. A recombinant human protein, hSRP1 alpha, bound in vitro specifically and directly to substrates containing either a simple or bipartite NLS motif. hSRP1 alpha promoted docking of import substrates to the nuclear envelope and together with recombinant human Ran reconstituted complete nuclear protein import. Thus, hSRP1 alpha has the properties of a cytosolic receptor for both simple and bipartite NLS motifs.


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Nuclear Localization and Export Signals of the Human Aryl Hydrocarbon Receptor.
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A T42A Ran Mutation: Differential Interactions with Effectors and Regulators, and Defect in Nuclear Protein Import.
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Ran-unassisted Nuclear Migration of a 97-kD Component of Nuclear Pore-targeting Complex.
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J. Cell Biol. 139, 841-849
   Abstract »    Full Text »    PDF »
Nucleocytoplasmic Recycling of the Nuclear Localization Signal Receptor {alpha} Subunit In Vivo Is Dependent on a Nuclear Export Signal, Energy, and RCC1.
I. Boche and E. Fanning (1997)
J. Cell Biol. 139, 313-325
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Differential Modes of Nuclear Localization Signal (NLS) Recognition by Three Distinct Classes of NLS Receptors.
Y. Miyamoto, N. Imamoto, T. Sekimoto, T. Tachibana, T. Seki, S. Tada, T. Enomoto, and Y. Yoneda (1997)
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Evidence for a Role of CRM1 in Signal-Mediated Nuclear Protein Export.
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Transportin-mediated Nuclear Import of Heterogeneous Nuclear RNP Proteins.
M. C. Siomi, P. S. Eder, N. Kataoka, L. Wan, Q. Liu, and G. Dreyfuss (1997)
J. Cell Biol. 138, 1181-1192
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M. Floer, G. Blobel, and M. Rexach (1997)
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J. Biol. Chem. 272, 6818-6822
   Abstract »    Full Text »    PDF »
Differential Expression and Sequence-specific Interaction of Karyopherin alpha with Nuclear Localization Sequences.
S. G. Nadler, D. Tritschler, O. K. Haffar, J. Blake, A. G. Bruce, and J. S. Cleaveland (1997)
J. Biol. Chem. 272, 4310-4315
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Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta.
R. Fridell, R Truant, L Thorne, R. Benson, and B. Cullen (1997)
J. Cell Sci. 110, 1325-1331
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Ran-binding Protein 1(RanBP1) Forms a Ternary Complex with Ran and Karyopherin beta and Reduces Ran GTPase-activating Protein (RanGAP) Inhibition by Karyopherin beta.
K. M. Lounsbury and I. G. Macara (1997)
J. Biol. Chem. 272, 551-555
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The Nuclear Localization Sequences of the BRCA1 Protein Interact with the Importin-alpha Subunit of the Nuclear Transport Signal Receptor.
C.-F. Chen, S. Li, Y. Chen, P.-L. Chen, Z. D. Sharp, and W.-H. Lee (1996)
J. Biol. Chem. 271, 32863-32868
   Abstract »    Full Text »    PDF »
Interferon-gamma -dependent Nuclear Import of Stat1 Is Mediated by the GTPase Activity of Ran/TC4.
T. Sekimoto, K. Nakajima, T. Tachibana, T. Hirano, and Y. Yoneda (1996)
J. Biol. Chem. 271, 31017-31020
   Abstract »    Full Text »    PDF »



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