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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-2-6
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pubmed:abstractText |
Many nuclear proteins are imported into the cell nucleus by the "classical" nuclear localization signal (NLS)-mediated import pathway. In this pathway, a sequence rich in basic residues in the protein interacts with a heterodimeric complex termed importin and this, along with the GTPase Ran, mediates nuclear import of the NLS-bearing protein. The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein contains a novel nuclear localization sequence, termed M9, that does not contain any clusters of basic residues. Very recently, we showed that M9 directs import into the nucleus by a novel protein import pathway distinct from the classical NLS pathway. A 90-kilodalton protein termed transportin was identified as a protein that specifically interacts with wild-type M9 but not transport-defective M9 mutants. Transportin and an ATP-regenerating system were found to be necessary and sufficient for import of M9-containing proteins in an in vitro import assay. In this report, we provide additional evidence that transportin can interact directly with M9-containing proteins and also show that it can mediate import of full-length hnRNP A1. In addition, Ran, or a Ran-binding protein, is identified as a second protein component of this novel nuclear import pathway. Transportin relatives from Saccharomyces cerevisiae which likely serve as additional nuclear transport receptors are described.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/hnRNP A1,
http://linkedlifedata.com/resource/pubmed/chemical/ran GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
229
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
261-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8986607-Amino Acid Sequence,
pubmed-meshheading:8986607-Animals,
pubmed-meshheading:8986607-Biological Transport, Active,
pubmed-meshheading:8986607-GTP Phosphohydrolases,
pubmed-meshheading:8986607-HeLa Cells,
pubmed-meshheading:8986607-Heterogeneous-Nuclear Ribonucleoprotein Group A-B,
pubmed-meshheading:8986607-Heterogeneous-Nuclear Ribonucleoproteins,
pubmed-meshheading:8986607-Humans,
pubmed-meshheading:8986607-Karyopherins,
pubmed-meshheading:8986607-Models, Biological,
pubmed-meshheading:8986607-Molecular Sequence Data,
pubmed-meshheading:8986607-Nuclear Localization Signals,
pubmed-meshheading:8986607-Nuclear Proteins,
pubmed-meshheading:8986607-Rabbits,
pubmed-meshheading:8986607-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:8986607-Ribonucleoproteins,
pubmed-meshheading:8986607-Saccharomyces cerevisiae,
pubmed-meshheading:8986607-Sequence Homology, Amino Acid,
pubmed-meshheading:8986607-ran GTP-Binding Protein
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pubmed:year |
1996
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pubmed:articleTitle |
Transportin: nuclear transport receptor of a novel nuclear protein import pathway.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania, 19104-6148, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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