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dc.contributor.author
Weßbecher, Isabel M.
dc.contributor.author
Hinrichsen, Inga
dc.contributor.author
Funke, Sebastian
dc.contributor.author
Oellerich, Thomas
dc.contributor.author
Plotz, Guido
dc.contributor.author
Zeuzem, Stefan
dc.contributor.author
Grus, Franz H.
dc.contributor.author
Biondi, Ricardo Miguel
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dc.contributor.author
Brieger, Angela
dc.date.available
2019-11-12T19:37:37Z
dc.date.issued
2018-12
dc.identifier.citation
Weßbecher, Isabel M.; Hinrichsen, Inga; Funke, Sebastian; Oellerich, Thomas; Plotz, Guido; et al.; DNA mismatch repair activity of MutLα is regulated by CK2-dependent phosphorylation of MLH1 (S477); Wiley-liss, Div John Wiley & Sons Inc; Molecular Carcinogenesis; 57; 12; 12-2018; 1723-1734
dc.identifier.issn
0899-1987
dc.identifier.uri
http://hdl.handle.net/11336/88677
dc.description.abstract
MutLα, a heterodimer consisting of MLH1 and PMS2, is a key player of DNA mismatch repair (MMR), yet little is known about its regulation. In this study, we used mass spectrometry to identify phosphorylated residues within MLH1 and PMS2. The most frequently detected phosphorylated amino acid was serine 477 of MLH1. Pharmacological treatment indicates that Casein kinase II (CK2) could be responsible for the phosphorylation of MLH1 at serine 477 in vivo. In vitro kinase assay verified MLH1 as a substrate of CK2. Most importantly, using in vitro MMR assay we could demonstrate that p-MLH1S477 lost MMR activity. Moreover, we found that levels of p-MLH1S477 varied during the cell cycle. In summary, we identified that phosphorylation of MLH1 by CK2 at amino acid position 477 can switch off MMR activity in vitro. Since CK2 is overexpressed in many tumors and is able to inactivate MMR, the new mechanism here described could have an important impact on tumors overactive in CK2.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley-liss, Div John Wiley & Sons Inc
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CK2
dc.subject
DNA MISMATCH REPAIR
dc.subject
LYNCH SYNDROME
dc.subject
MLH1
dc.subject
MUTLΑ
dc.subject
PHOSPHORYLATION
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
DNA mismatch repair activity of MutLα is regulated by CK2-dependent phosphorylation of MLH1 (S477)
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-22T17:53:54Z
dc.journal.volume
57
dc.journal.number
12
dc.journal.pagination
1723-1734
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Weßbecher, Isabel M.. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Hinrichsen, Inga. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Funke, Sebastian. Klinikum Der Johannes-gutenberg-universität Und Fachbereich Medizin; Alemania
dc.description.fil
Fil: Oellerich, Thomas. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Plotz, Guido. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Zeuzem, Stefan. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Grus, Franz H.. Klinikum Der Johannes-gutenberg-universität Und Fachbereich Medizin; Alemania
dc.description.fil
Fil: Biondi, Ricardo Miguel. Goethe Universitat Frankfurt; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Brieger, Angela. Goethe Universitat Frankfurt; Alemania
dc.journal.title
Molecular Carcinogenesis
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/mc.22892
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/mc.22892
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