Title: In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import.
Abstract: Research Article1 August 1995free access In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import. N. Imamoto N. Imamoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Shimamoto T. Shimamoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Takao T. Takao Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Tachibana T. Tachibana Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author S. Kose S. Kose Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author M. Matsubae M. Matsubae Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Sekimoto T. Sekimoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author Y. Shimonishi Y. Shimonishi Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author Y. Yoneda Y. Yoneda Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author N. Imamoto N. Imamoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Shimamoto T. Shimamoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Takao T. Takao Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Tachibana T. Tachibana Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author S. Kose S. Kose Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author M. Matsubae M. Matsubae Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author T. Sekimoto T. Sekimoto Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author Y. Shimonishi Y. Shimonishi Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author Y. Yoneda Y. Yoneda Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. Search for more papers by this author Author Information N. Imamoto1, T. Shimamoto1, T. Takao1, T. Tachibana1, S. Kose1, M. Matsubae1, T. Sekimoto1, Y. Shimonishi1 and Y. Yoneda1 1Department of Anatomy and Cell Biology, Osaka University Medical School, Japan. The EMBO Journal (1995)14:3617-3626https://doi.org/10.1002/j.1460-2075.1995.tb00031.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We recently showed that a nuclear location signal (NLS)-containing karyophile forms a stable complex with cytoplasmic components for nuclear pore-targeting The complex, termed nuclear pore-targeting complex (PTAC), contained two essential proteins of 54 and 90 kDa, respectively, as estimated by electrophoresis. In this study, we found that the 54 kDa component of PTAC is the mouse homologue of Xenopus importin (m-importin). Cytoplasmic injection of the antibodies raised against recombinant m-importin showed an inhibitory effect on nuclear import of a karyophile in living mammalian cells. A portion of cytoplasmically injected antibodies migrated rapidly into the nucleus, indicating dynamic movement of this protein across the nuclear envelope. Moreover, the injected antibodies co-precipitated the karyophile, in an NLS-dependent manner, with endogenous m-importin in the cytoplasm. These results provide in vivo evidence that m-importin is involved in nuclear protein import through association with a NLS in the cytoplasm before nuclear pore binding. Previous ArticleNext Article Volume 14Issue 151 August 1995In this issue RelatedDetailsLoading ...