Characterization of the nuclear transport of a novel leucine‐rich acidic nuclear protein‐like protein

FEBS Letters

Kurihara, Toshinao²  Tachibana, Taro¹  Yoneda, Yoshihiro²  Imamoto, Naoko²  Matsubae, Masami² 

[1] Department of Neuroscience, Biomedical Research Center, Graduate School of Medicine, Osaka University, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan;Department of Cell Biology and Neuroscience, Osaka University, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan

关键词: Nuclear protein import;    Nuclear localization signal;    Importin α;    Leucine-rich acidic nuclear protein;    Ataxin-1;    NLS;    nuclear localization signal;    WGA;    wheat germ agglutinin;    LANP;    leucine-rich acidic nuclear protein;    NPC;    nuclear pore complex;   

DOI  :  10.1016/S0014-5793(00)01218-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α. These findings suggest that mLANP-L is transported into the nucleus by Rch1 and/or NPI-1.

【 授权许可】

Unknown