Abstract
The mitotic kinesin-like protein (Mklp-1) localizes in the nucleus during interphase due to the presence of nuclear localization signal(s) [NLS(s)] within its sequence. Here, we mapped two NLSs to be 899SRKRRSST906 and 949KRKKP953 in the tail domain of Mklp-1, and showed that ectopic expression of a mutant Mklp-1 without the NLSs leads to cell cycle arrest at cytokinesis, indicating that the NLSs are necessary for Mklp-1 to execute its normal function during cell division. Furthermore, mutation of two serine residues in the first NLS to aspartic acid, which mimics phosphorylation, attenuated its nuclear localization function, suggesting that the function of this NLS might be regulated by phosphorylation.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Blotting, Western
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Cell Cycle / genetics
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Cell Cycle / physiology
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Cell Cycle Proteins / metabolism
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Cytokinesis / genetics
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Cytokinesis / physiology*
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Fluorescent Antibody Technique
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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HeLa Cells
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Humans
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Microtubule-Associated Proteins / genetics
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Microtubule-Associated Proteins / metabolism
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Microtubule-Associated Proteins / physiology*
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Mutation*
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Nuclear Localization Signals / genetics*
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Phosphorylation
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Polo-Like Kinase 1
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Protein Serine-Threonine Kinases / metabolism
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Proto-Oncogene Proteins / metabolism
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Transfection
Substances
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Cell Cycle Proteins
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KIF23 protein, human
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Microtubule-Associated Proteins
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Nuclear Localization Signals
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins
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Green Fluorescent Proteins
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Protein Serine-Threonine Kinases