Characterization of the nuclear transport of a novel leucine-rich acidic nuclear protein-like protein |
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Authors: | Matsubae M Kurihara T Tachibana T Imamoto N Yoneda Y |
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Affiliation: | Department of Cell Biology, Osaka University, 2-2 Yamada-oka, Suita, Osaka, Japan. |
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Abstract: | We previously reported that the nuclear localization signal (NLS) peptides stimulate the in vitro phosphorylation of several proteins, including a 34 kDa protein. In this study, we show that this specific 34 kDa protein is a novel murine leucine-rich acidic nuclear protein (LANP)-like large protein (mLANP-L). mLANP-L was found to have a basic type NLS. The co-injection of Q69LRan-GTP or SV40 T-antigen NLS peptides prevented the nuclear import of mLANP-L. mLANP-L NLS bound preferentially to Rch1 and NPI-1, but not to the Qip1 subfamily of importin alpha. These findings suggest that mLANP-L is transported into the nucleus by Rch1 and/or NPI-1. |
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