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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-3-8
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pubmed:abstractText |
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 complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0962-8924
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
121-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15752974-Active Transport, Cell Nucleus,
pubmed-meshheading:15752974-Amino Acid Sequence,
pubmed-meshheading:15752974-Animals,
pubmed-meshheading:15752974-Binding Sites,
pubmed-meshheading:15752974-Cell Nucleus,
pubmed-meshheading:15752974-Cytoplasm,
pubmed-meshheading:15752974-Humans,
pubmed-meshheading:15752974-Karyopherins,
pubmed-meshheading:15752974-Leucine,
pubmed-meshheading:15752974-Models, Biological,
pubmed-meshheading:15752974-Molecular Sequence Data,
pubmed-meshheading:15752974-Nuclear Pore,
pubmed-meshheading:15752974-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:15752974-Sequence Homology, Amino Acid,
pubmed-meshheading:15752974-Signal Transduction
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pubmed:year |
2005
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pubmed:articleTitle |
Leucine-rich nuclear-export signals: born to be weak.
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pubmed:affiliation |
Swiss Federal Institute of Technology (ETH) Zürich, Institute of Biochemistry, Schafmattstrasse 18, HPM F11.1, 8093 Zürich, Switzerland. ulrike.kutay@bc.biol.ethz.ch
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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