Identification and characterization of a nuclear pore complex protein |
| |
| Authors: | L I Davis G Blobel |
| |
| Affiliation: | 1. Department of Stem Cell Biology, School of Medicine, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea;2. Department of Animal Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea;3. Dong-A Socio Holdings Research Center, 21, Geumhwa-ro 105 beon-gil, Giheung-gu, Yongin-si, Republic of Korea;4. Department of Cell and Developmental Biology, Max Planck Institute for Molecular Biomedicine, Röntgenstraße 20, 48149 Münster, Germany;5. University of Münster, Medical Faculty, Domagkstraße 3, 48149 Münster, Germany;6. Animal Biotechnology Division, National Institute of Animal Science, RDA, Suwon 441-706, Republic of Korea;7. School of Life Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, Republic of Korea;8. KU Open-Innovation Center, Institute of Biomedical Science & Technology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea |
| |
| Abstract: | We describe studies using a monoclonal antibody that recognizes a 62 kd protein (p62) of rat liver nuclei. This protein remains associated with the nuclear pore complex-lamina fraction resulting from treatment of nuclei with DNAase, RNAase, and nonionic detergent. Immunofluorescence revealed a strikingly punctate pattern of nuclear rim staining. By immunoferritin microscopy, p62 was specifically localized to the pore complex. Thus, pore complexes can be resolved by fluorescence light microscopy. Pulse chase analysis of labeled tissue culture cells showed that p62 is synthesized as a soluble cytoplasmic precursor of 61 kd, which is incorporated into the nuclear fraction with an unusually long t1/2 of about 6 hr. Incorporation is followed by modification that may involve addition of N-acetylglucosamine residues. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
