A Distinct Nuclear Import Pathway Used by Ribosomal Proteins

Protein transport into the nucleus is governed by the interaction of soluble transport factors with their import substrates and nuclear pore complexes. Here, we identify a major distinct nuclear import pathway, mediated by a previously uncharacterized yeast β karyopherin Kap123p. The predominant sub...

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Bibliographic Details
Published inCell Vol. 89; no. 5; pp. 715 - 725
Main Authors Rout, Michael P, Blobel, Günter, Aitchison, John D
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.05.1997
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Summary:Protein transport into the nucleus is governed by the interaction of soluble transport factors with their import substrates and nuclear pore complexes. Here, we identify a major distinct nuclear import pathway, mediated by a previously uncharacterized yeast β karyopherin Kap123p. The predominant substrates for this pathway are ribosomal proteins, which must be imported into the nucleus prior to assembly into preribosomes. Kap123p binds directly to its transport substrates, repeat motif–containing nucleoporins, and Ran-GTP. We show that the related protein Pse1p is also a karyopherin and can functionally substitute for Kap123p; both are capable of specifically directing a ribosomal nuclear localization signal reporter to the nucleus in vivo.
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ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)80254-8