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Cyclin E-dependent localization of MCM5 regulates centrosome duplication
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Cell Science, 121, 2008, 19, S. 3224-3232 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
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Ferguson, Rebecca L. Maller, James L. Ferguson, Rebecca L. Maller, James L. |
|---|---|
| author |
Ferguson, Rebecca L. Maller, James L. |
| spellingShingle |
Ferguson, Rebecca L. Maller, James L. Journal of Cell Science Cyclin E-dependent localization of MCM5 regulates centrosome duplication Cell Biology |
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ferguson, rebecca l. |
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Ferguson, Rebecca L. Maller, James L. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.034702 <jats:p>Centrosomes are the primary microtubule-organizing centers in animal cells and are required for bipolar spindle assembly during mitosis. Amplification of centrosome number is commonly observed in human cancer cells and might contribute to genomic instability. Cyclin E–Cdk2 has been implicated in regulating centrosome duplication both in Xenopus embryos and extracts and in mammalian cells. Localization of cyclin E on centrosomes is mediated by a 20-amino acid domain termed the centrosomal localization sequence (CLS). In this paper, cyclin E is shown to directly interact with and colocalize on centrosomes with the DNA replication factor MCM5 in a CLS-dependent but Cdk2-independent manner. The domain in MCM5 that is responsible for interaction with cyclin E is distinct from any previously described for MCM5 function and is highly conserved in MCM5 proteins from yeast to mammals. Expression of MCM5 or its cyclin E-interacting domain, but not MCM2, significantly inhibits over-duplication of centrosomes in CHO cells arrested in S-phase. These results indicate that proteins involved in DNA replication might also regulate centrosome duplication.</jats:p> Cyclin E-dependent localization of MCM5 regulates centrosome duplication Journal of Cell Science |
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Journal of Cell Science |
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| title |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_unstemmed |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_full |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_fullStr |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_full_unstemmed |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_short |
Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_sort |
cyclin e-dependent localization of mcm5 regulates centrosome duplication |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.034702 |
| publishDate |
2008 |
| physical |
3224-3232 |
| description |
<jats:p>Centrosomes are the primary microtubule-organizing centers in animal cells and are required for bipolar spindle assembly during mitosis. Amplification of centrosome number is commonly observed in human cancer cells and might contribute to genomic instability. Cyclin E–Cdk2 has been implicated in regulating centrosome duplication both in Xenopus embryos and extracts and in mammalian cells. Localization of cyclin E on centrosomes is mediated by a 20-amino acid domain termed the centrosomal localization sequence (CLS). In this paper, cyclin E is shown to directly interact with and colocalize on centrosomes with the DNA replication factor MCM5 in a CLS-dependent but Cdk2-independent manner. The domain in MCM5 that is responsible for interaction with cyclin E is distinct from any previously described for MCM5 function and is highly conserved in MCM5 proteins from yeast to mammals. Expression of MCM5 or its cyclin E-interacting domain, but not MCM2, significantly inhibits over-duplication of centrosomes in CHO cells arrested in S-phase. These results indicate that proteins involved in DNA replication might also regulate centrosome duplication.</jats:p> |
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| author | Ferguson, Rebecca L., Maller, James L. |
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| description | <jats:p>Centrosomes are the primary microtubule-organizing centers in animal cells and are required for bipolar spindle assembly during mitosis. Amplification of centrosome number is commonly observed in human cancer cells and might contribute to genomic instability. Cyclin E–Cdk2 has been implicated in regulating centrosome duplication both in Xenopus embryos and extracts and in mammalian cells. Localization of cyclin E on centrosomes is mediated by a 20-amino acid domain termed the centrosomal localization sequence (CLS). In this paper, cyclin E is shown to directly interact with and colocalize on centrosomes with the DNA replication factor MCM5 in a CLS-dependent but Cdk2-independent manner. The domain in MCM5 that is responsible for interaction with cyclin E is distinct from any previously described for MCM5 function and is highly conserved in MCM5 proteins from yeast to mammals. Expression of MCM5 or its cyclin E-interacting domain, but not MCM2, significantly inhibits over-duplication of centrosomes in CHO cells arrested in S-phase. These results indicate that proteins involved in DNA replication might also regulate centrosome duplication.</jats:p> |
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| spelling | Ferguson, Rebecca L. Maller, James L. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.034702 <jats:p>Centrosomes are the primary microtubule-organizing centers in animal cells and are required for bipolar spindle assembly during mitosis. Amplification of centrosome number is commonly observed in human cancer cells and might contribute to genomic instability. Cyclin E–Cdk2 has been implicated in regulating centrosome duplication both in Xenopus embryos and extracts and in mammalian cells. Localization of cyclin E on centrosomes is mediated by a 20-amino acid domain termed the centrosomal localization sequence (CLS). In this paper, cyclin E is shown to directly interact with and colocalize on centrosomes with the DNA replication factor MCM5 in a CLS-dependent but Cdk2-independent manner. The domain in MCM5 that is responsible for interaction with cyclin E is distinct from any previously described for MCM5 function and is highly conserved in MCM5 proteins from yeast to mammals. Expression of MCM5 or its cyclin E-interacting domain, but not MCM2, significantly inhibits over-duplication of centrosomes in CHO cells arrested in S-phase. These results indicate that proteins involved in DNA replication might also regulate centrosome duplication.</jats:p> Cyclin E-dependent localization of MCM5 regulates centrosome duplication Journal of Cell Science |
| spellingShingle | Ferguson, Rebecca L., Maller, James L., Journal of Cell Science, Cyclin E-dependent localization of MCM5 regulates centrosome duplication, Cell Biology |
| title | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_full | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_fullStr | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_full_unstemmed | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_short | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| title_sort | cyclin e-dependent localization of mcm5 regulates centrosome duplication |
| title_unstemmed | Cyclin E-dependent localization of MCM5 regulates centrosome duplication |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.034702 |