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...
Saved in:
Published in | Cell Vol. 89; no. 5; pp. 715 - 725 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
30.05.1997
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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. |
---|---|
Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0092-8674 1097-4172 |
DOI: | 10.1016/S0092-8674(00)80254-8 |