Cited by 219Nuclear Structure and FunctionRNA Research and SplicingDrug Transport and Resistance Mechanisms

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The Specificity of the CRM1-Rev Nuclear Export Signal Interaction Is Mediated by RanGTP

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Askjaer, Peter, Jensen, Torben Heick, Nilsson, Jakob, Englmeier, Ludwig, Kjems, Jørgen·1998·Journal of Biological Chemistry

DOI 10.1074/jbc.273.50.33414

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Abstract

Nuclear export of intron-containing human immunodeficiency virus type 1 (HIV-1) RNA is mediated by the viral Rev protein that contains both an RNA binding domain specific for the viral Rev response element (RRE) and a nuclear export signal (NES). The cellular CRM1 (Exportin1) protein functions as a nuclear export receptor for proteins carrying a Rev-like NES in a process that also requires the GTP bound form of the Ran GTPase. Using purified recombinant factors, we show by co-precipitation, gel mobility shift and protein footprinting assays that full-length Rev protein interacts directly with CRM1 in vitro independently of both the integrity of the characteristic leucine residues of the NES and the presence of the cytotoxin leptomycin B (LMB). Addition of RanGTP induces the formation of an RRE-Rev-CRM1-RanGTP complex that is sensitive to LMB, NES mutations, and Ran being charged with GTP. Within this complex, CRM1 is readily cross-linked to Cys89 near the NES of Rev. By protein footprinting, we demonstrate that the NES of Rev and two regions in CRM1 become inaccessible to endoproteinases upon binding suggesting that these regions are involved in protein-protein interactions. Our data are consistent with a model in which CRM1 is the nuclear export receptor for the Rev-RRE ribonucleoprotein complex and that RanGTP binds to a preformed Rev-CRM1 complex and specifies a functional interaction with the NES.

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CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086
CRM1 is responsible for intracellular transport mediated by the nuclear export signal
Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M., & Nishida, E. (1997) · Nature · doi:10.1038/36894 · Cited by 1,213
Identification of a signal for rapid export of proteins from the nucleus
Wen, W., Meinkotht, J. L., Tsien, R. Y., & Taylor, S. S. (1995) · Cell · doi:10.1016/0092-8674(95)90435-2 · Cited by 1,190
Nucleocytoplasmic transport: the soluble phase
Mattaj, I. W., & Englmeier, L. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.265 · Cited by 1,175
Self-citation
Exportin 1 (Crm1p) Is an Essential Nuclear Export Factor
Stade, K., Ford, C. S., Guthrie, C., & Weis, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80370-0 · Cited by 1,145
The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W., & Lührmann, R. (1995) · Cell · doi:10.1016/0092-8674(95)90436-0 · Cited by 1,140
Functional dissection of the HIV-1 Rev trans-activator—Derivation of a trans-dominant repressor of Rev function
Malim, M. H., Böhnlein, S., Hauber, J., & Cullen, B. R. (1989) · Cell · doi:10.1016/0092-8674(89)90416-9 · Cited by 732
Evidence for a Role of CRM1 in Signal-Mediated Nuclear Protein Export
Ossareh‐Nazari, B., Bachelerie, F., & Dargemont, C. (1997) · Science · doi:10.1126/science.278.5335.141 · Cited by 713
Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
Bischoff, F. R., & Ponstingl, H. (1991) · Nature · doi:10.1038/354080a0 · Cited by 711
Isolation of a protein that is essential for the first step of nuclear protein import
Görlich, D. (1994) · Cell · doi:10.1016/0092-8674(94)90067-1 · Cited by 695

Show all 49 references

Research works printed but not linked: 5

Kalland, 1994, Mol. Cell. Biol., 14, 7436
Perkins, 1989, J. Acquired Immune Defic. Syndr., 2, 256
Fankhauser, 1991, Mol. Cell. Biol., 11, 2567
Olsen, 1991, J. Acquired Immune Defic. Syndr., 4, 558
Izaurralde, 1998, RNA, 4, 351

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Authors: Askjaer, P., Jensen, T. H., Nilsson, J., Englmeier, L., & Kjems, J.
Affiliations: Aarhus University (DK)
Corresponding author: Kjems, Jørgen
ORCID: Askjaer, Peter
Jensen, Torben Heick
Nilsson, Jakob
Englmeier, Ludwig
Kjems, Jørgen
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1998-12
Volume: 273
Issue: 50
Pages: 33414-33422
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.273.50.33414
OpenAlex: W1979451022
Cited by: 219
References: 49
Citations by year: 2026: 2 · 2025: 3 · 2024: 6 · 2023: 2 · 2022: 7 · 2021: 3 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 3 · 2016: 6 · 2015: 5 · 2014: 10 · 2013: 8 · 2012: 16
FWCI: 4.83
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7979 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Kræftens Bekæmpelse
Karen Elise Jensens Fond
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords: CRM1, Rev protein, nuclear export signal, Ran GTPase, Rev response element, protein-protein interaction, leptomycin B, nuclear export receptor
MeSH terms: Exportin 1 Protein, Base Sequence, Carrier Proteins, Cell Nucleus, Guanosine Triphosphate, Recombinant Proteins, Ultraviolet Rays, Signal Transduction, Gene Products, rev, DNA Primers, Receptors, Cytoplasmic and Nuclear, Karyopherins

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The Specificity of the CRM1-Rev Nuclear Export Signal Interaction Is Mediated by RanGTP

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