Display Settings:

Format

Send to:

Choose Destination
Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4451-6.

Cloning and characterization of human karyopherin beta3.

Author information

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA.

Abstract

Nuclear import of classical nuclear localization sequence-bearing proteins is mediated by karyopherin alpha/beta1 heterodimers. A second nuclear import pathway, mediated by karyopherin beta2 (transportin), recently was described for mRNA-binding proteins. Here we report the cloning and characterization of human karyopherin beta3, which may be involved in a third pathway for nuclear import. Karyopherin beta3 was localized mainly to the cytosol and the nucleus, particularly the nuclear rim. It bound to several of the repeat-containing nucleoporins (Nup358, Nup214, Nup153, Nup98, and p62) in overlay and solution-binding assays and was competed away by karyopherin beta1. For Nup98, we localized this binding to the peptide repeat-containing region. Karyopherin beta3 contains two putative Ran-binding homology regions and bound to Ran-GTP in a solution-binding assay with much higher affinity than to Ran-GDP. Furthermore, it interacted with two ribosomal proteins in an overlay assay. We suggest that karyopherin beta3 is a nuclear transport factor that may mediate the import of some ribosomal proteins into the nucleus.

PMID:
9114010
[PubMed - indexed for MEDLINE]
PMCID:
PMC20743
Free PMC Article

Images from this publication.See all images (6)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk