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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Antigens, Polyomavirus Transforming / metabolism
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Cell Nucleus / metabolism*
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Cloning, Molecular
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Green Fluorescent Proteins
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HeLa Cells
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Humans
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Luminescent Proteins / genetics
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Male
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Mice
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Mice, Inbred C57BL
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Molecular Sequence Data
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Molecular Weight
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Mutagenesis, Site-Directed
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Neuropeptides / chemistry
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Neuropeptides / genetics
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Neuropeptides / metabolism*
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Phosphorylation
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Rats
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Transfection
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ran GTP-Binding Protein / metabolism
Substances
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ANP32B protein, human
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Anp32a protein, rat
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Antigens, Polyomavirus Transforming
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Luminescent Proteins
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Neuropeptides
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Nuclear Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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Green Fluorescent Proteins
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ran GTP-Binding Protein