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dc.contributor.authorRoesner, Lennart M
dc.contributor.authorMielke, Christian
dc.contributor.authorFaehnrich, Silke
dc.contributor.authorMerkhoffer, Yvonne
dc.contributor.authorDittmar, Kurt E J
dc.contributor.authorDrexler, Hans G
dc.contributor.authorDirks, Wilhelm G
dc.date.accessioned2014-10-13T14:10:38Z
dc.date.available2014-10-13T14:10:38Z
dc.date.issued2014
dc.identifier.citationLocalization of MLH3 at the centrosomes. 2014, 15 (8):13932-7 Int J Mol Scien
dc.identifier.issn1422-0067
dc.identifier.pmid25116689
dc.identifier.doi10.3390/ijms150813932
dc.identifier.urihttp://hdl.handle.net/10033/332725
dc.description.abstractMutations in human DNA mismatch repair (MMR) genes are commonly associated with hereditary nonpolyposis colorectal cancer (HNPCC). MLH1 protein heterodimerizes with PMS2, PMS1, and MLH3 to form MutLα, MutLβ, and MutLγ, respectively. We reported recently stable expression of GFP-linked MLH3 in human cell lines. Monitoring these cell lines during the cell cycle using live cell imaging combined with confocal microscopy, we detected accumulation of MLH3 at the centrosomes. Fluorescence recovery after photobleaching (FRAP) revealed high mobility and fast exchange rates at the centrosomes as it has been reported for other DNA repair proteins. MLH3 may have a role in combination with other repair proteins in the control of centrosome numbers.
dc.language.isoenen
dc.rightsArchived with thanks to International journal of molecular sciencesen
dc.titleLocalization of MLH3 at the centrosomes.en
dc.typeArticleen
dc.identifier.journalInternational journal of molecular sciencesen
refterms.dateFOA2018-06-13T01:30:29Z
html.description.abstractMutations in human DNA mismatch repair (MMR) genes are commonly associated with hereditary nonpolyposis colorectal cancer (HNPCC). MLH1 protein heterodimerizes with PMS2, PMS1, and MLH3 to form MutLα, MutLβ, and MutLγ, respectively. We reported recently stable expression of GFP-linked MLH3 in human cell lines. Monitoring these cell lines during the cell cycle using live cell imaging combined with confocal microscopy, we detected accumulation of MLH3 at the centrosomes. Fluorescence recovery after photobleaching (FRAP) revealed high mobility and fast exchange rates at the centrosomes as it has been reported for other DNA repair proteins. MLH3 may have a role in combination with other repair proteins in the control of centrosome numbers.


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