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Crystallization of Nuclear Export Signals or Small-Molecule Inhibitors Bound to Nuclear Exporter CRM1

2022
The Karyopherin protein CRM1 or XPO1 is the major nuclear export receptor that regulates nuclear exit of thousands of macromolecules in the cell. CRM1 recognizes protein cargoes by binding to their 8-15 residue-long nuclear export signals (NESs). A ternary CRM1-Ran-RanBP1 complex engineered to be suitable for crystallization has enabled structure ...
Ho Yee Joyce, Fung, Yuh Min, Chook
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Binding Affinity Measurement of Nuclear Export Signal Peptides to Their Exporter CRM1

2022
CRM1 recognizes hundreds to thousands of protein cargoes by binding to the eight to fifteen residue-long nuclear export signals (NESs) within their polypeptide chains. Various assays to measure the binding affinity of NESs for CRM1 have been developed.
Ho Yee Joyce, Fung, Yuh Min, Chook
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Nuclear Import and Export Signals

2007
Eukaryotic cells are separated into two large compartments, namely the nucleus and the cytoplasm, by the nuclear envelope. As a result, macromolecules including RNAs, which are transcribed in the nucleus and nuclear proteins, which are translated in the cytoplasm must cross the double Upid bilayer to reach the intracellular sites where they function ...
Toshihiro Sekimoto   +2 more
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Signal transduction meets nuclear export

Trends in Cell Biology, 1998
Abstract ENGEL, K. et al . (1998) Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation EMBO J.
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Nuclear import-export: In search of signals and mechanisms

Cell, 1991
E. A. Nigg,’ P. A. Baeuerle,t and R. LiihrmannS *Swiss Institute for Experimental Cancer Research CH-1066 Epalinges Switzerland TGenzentrum der Ludwig-Maximilians-Universitkt D-8033 Martinsried Germany *lnstitut fiir Molekularbiologie und Tumorforschung Universitat Marburg D-3550 Marburg Germany In eukaryotic cells, there is continuous exchange of ...
Nigg, E. A.   +2 more
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Leucine-rich nuclear-export signals: born to be weak

Trends in Cell Biology, 2005
CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore ...
Ulrike, Kutay, Stephan, Güttinger
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Nuclear export of α-catenin: overlap between nuclear export signal sequences and the β-catenin binding site

Experimental Cell Research, 2004
Mutations in APC or in beta-catenin, which are common in colon cancer, lead to constitutive activation of beta-catenin/Tcf-dependent signaling. alpha-Catenin is also found in some colon cancer cell nuclei, and loss of its expression correlates with increased beta-catenin/Tcf transcriptional activity.
Giannini, A   +5 more
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Nuclear-localization-signal-dependent and nuclear-export-signal-dependent mechanisms determine the localization of 5-lipoxygenase

Biochemical Journal, 2002
5-Lipoxygenase (5-LO) metabolizes arachidonic acid to leukotriene A4, a key intermediate in leukotriene biosynthesis. To explore the molecular mechanisms of its cell-specific localization, a fusion protein between green fluorescent protein (GFP) and human 5-LO (GFP—5LO) was expressed in various cells. GFP—5LO was localized in the cytosol in HL-60 cells
Hiromi, Hanaka   +2 more
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Targeting The Nuclear Export Signal In Multiple Myeloma

Blood, 2013
Abstract Introduction In multiple myeloma (MM), de novo drug resistance to topoisomerase (topo) II poisons occurs at high cell densities due to trafficking of topo IIα from the nucleus to the cytoplasm where it is no longer in contact with the DNA and thus unable to induce cell death (Turner et al ...
Joel G Turner   +6 more
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