Characterization of the nuclear transport of a novel leucine‐rich acidic nuclear protein‐like protein
M Matsubae, T Kurihara, T Tachibana, N Imamoto… - FEBS …, 2000 - Wiley Online Library
M Matsubae, T Kurihara, T Tachibana, N Imamoto, Y Yoneda
FEBS letters, 2000•Wiley Online LibraryWe 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 …
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 …
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.
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