rdf:type |
|
lifeskim:mentions |
umls-concept:C0007610,
umls-concept:C0085862,
umls-concept:C0142661,
umls-concept:C0678594,
umls-concept:C1299583,
umls-concept:C1527178,
umls-concept:C1549571,
umls-concept:C1550548,
umls-concept:C1555714,
umls-concept:C1608386,
umls-concept:C1705654
|
pubmed:issue |
4
|
pubmed:dateCreated |
2008-2-13
|
pubmed:databankReference |
|
pubmed:abstractText |
The nuclear import of assembled spliceosomal subunits, the uridine-rich small nuclear ribonucleoprotein particles (U snRNPs), is mediated by a nuclear import receptor adaptor couple of importin beta (Imp beta) and snurportin1 (SPN1). In contrast to any other characterized active nuclear import, the Imp beta/SPN1/U snRNP complex does not require RanGTP for the terminal release from the nuclear basket of the nuclear pore complex (NPC). The crystal structure of Imp beta (127-876) in complex with the Imp beta-binding (IBB) domain of SPN1 (1-65) at 2.8-A resolution reveals that Imp beta adopts an open conformation, which is unique for a functional Imp beta/cargo complex, and rather surprisingly, it resembles the conformation of the Imp beta/RanGTP complex. As binding of RanGTP to Imp beta usually triggers the release of import complexes from the NPC, we propose that by already mimicking a conformation similar to Imp beta/RanGTP the independent dissociation of Imp beta/SPN1 from the nuclear basket is energetically aided.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1089-8638
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pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
7
|
pubmed:volume |
374
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1129-38
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pubmed:meshHeading |
pubmed-meshheading:18028944-Active Transport, Cell Nucleus,
pubmed-meshheading:18028944-Cell Nucleus,
pubmed-meshheading:18028944-Crystallography, X-Ray,
pubmed-meshheading:18028944-Humans,
pubmed-meshheading:18028944-Nuclear Pore,
pubmed-meshheading:18028944-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:18028944-Protein Binding,
pubmed-meshheading:18028944-RNA Cap-Binding Proteins,
pubmed-meshheading:18028944-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:18028944-Ribonucleoprotein, U1 Small Nuclear,
pubmed-meshheading:18028944-Spliceosomes,
pubmed-meshheading:18028944-beta Karyopherins,
pubmed-meshheading:18028944-ran GTP-Binding Protein
|
pubmed:year |
2007
|
pubmed:articleTitle |
Structural basis for RanGTP independent entry of spliceosomal U snRNPs into the nucleus.
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pubmed:affiliation |
Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik and GZMB, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|