Abstract
The human Nup107-160 nucleoporin complex plays a major role in formation of the nuclear pore complex and is localized to kinetochores in mitosis. Here we report that Seh1, a component of the Nup107-160 complex, functions in chromosome alignment and segregation by regulating the centromeric localization of Aurora B and other chromosome passenger complex proteins. Localization of CENP-E is not affected by Seh1 depletion and analysis by electron microscopy showed that microtubule kinetochore attachments are intact. Seh1-depleted cells show impaired Aurora B localization, which results in severe defects in biorientation and organization of the spindle midzone and midbody. Our results indicate that a major function of the Nup107 complex in mitosis is to ensure the proper localization of the CPC at the centromere.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anaphase / drug effects
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Aurora Kinase B
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Aurora Kinases
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Chromosome Segregation / drug effects
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Chromosomes, Human / drug effects
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Chromosomes, Human / metabolism*
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Chromosomes, Human / ultrastructure
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Cytokinesis / drug effects
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HeLa Cells
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Humans
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Kinesins / metabolism
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Kinetochores / drug effects
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Kinetochores / metabolism
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Kinetochores / ultrastructure
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Mitosis* / drug effects
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Nocodazole / pharmacology
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Nuclear Pore Complex Proteins / metabolism*
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Nuclear Proteins / metabolism*
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Paclitaxel / pharmacology
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Phosphorylation / drug effects
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Protein Serine-Threonine Kinases / metabolism
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Pyrimidines / metabolism
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Spindle Apparatus / drug effects
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Spindle Apparatus / metabolism
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Spindle Apparatus / ultrastructure
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Substrate Specificity / drug effects
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Thiones / metabolism
Substances
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KIF2C protein, human
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NUP107 protein, human
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NUP160 protein, human
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Nuclear Pore Complex Proteins
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Nuclear Proteins
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Pyrimidines
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Thiones
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monastrol
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AURKB protein, human
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Aurora Kinase B
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Aurora Kinases
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Protein Serine-Threonine Kinases
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Kinesins
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Paclitaxel
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Nocodazole