Quantitative comparison of a human cancer cell surface proteome between interphase and mitosis |
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Authors: | Mohammad H Qureshi Yusuke Toyoda Bernhard Y Renard Gürkan Mollaoglu Nazlı E Özkan Selda Bulbul Ina Poser Wiebke Timm Anthony A Hyman Timothy J Mitchison Judith A Steen |
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Affiliation: | 1.Department of Molecular Biology and Genetics, Koç University, Istanbul, Turkey;2.Proteomics Center at Children*s Hospital Boston, Boston, MA, USA;3.Department of Systems Biology, Harvard Medical School, Boston, MA, USA;4.Max Planck Institute for Molecular Cell Biology and Genetics, Dresden, Germany;5.Research Group Bioinformatics (NG 4), Robert Koch-Institute, Berlin, Germany;6.Department of Neurobiology, Harvard Medical School and Children*s Hospital Boston, Boston, MA, USA |
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Abstract: | The cell surface is the cellular compartment responsible for communication with the environment. The interior of mammalian cells undergoes dramatic reorganization when cells enter mitosis. These changes are triggered by activation of the CDK1 kinase and have been studied extensively. In contrast, very little is known of the cell surface changes during cell division. We undertook a quantitative proteomic comparison of cell surface‐exposed proteins in human cancer cells that were tightly synchronized in mitosis or interphase. Six hundred and twenty‐eight surface and surface‐associated proteins in HeLa cells were identified; of these, 27 were significantly enriched at the cell surface in mitosis and 37 in interphase. Using imaging techniques, we confirmed the mitosis‐selective cell surface localization of protocadherin PCDH7, a member of a family with anti‐adhesive roles in embryos. We show that PCDH7 is required for development of full mitotic rounding pressure at the onset of mitosis. Our analysis provided basic information on how cell cycle progression affects the cell surface. It also provides potential pharmacodynamic biomarkers for anti‐mitotic cancer chemotherapy. |
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Keywords: | cell cycle cell rounding cell surface PCDH7
SILAC
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