Human mutation · 2012
Functional characterization of MLH1 missense variants identified in Lynch syndrome patients.
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Andersen Sofie Dabros, Liberti Sascha Emilie, Lützen Anne, Drost Mark, Bernstein Inge, Nilbert Mef, Dominguez Mev, Nyström Minna, Hansen Thomas Van Overeem, Christoffersen Janus Wiese, Jäger Anne Charlotte, de Wind Niels, Nielsen Finn Cilius, Tørring Pernille M, Rasmussen Lene Juel
Аннотация
Germline mutations in the human DNA mismatch repair (MMR) genes MSH2 and MLH1 are associated with the inherited cancer disorder Lynch syndrome (LS), also known as hereditary nonpolyposis colorectal cancer or HNPCC. A proportion of MSH2 and MLH1 mutations found in suspected LS patients give rise to single amino acid substitutions. The functional consequences in regard to pathogenicity of many of these variants are unclear. We have examined the functionality of a panel of MLH1 missense mutations found in LS families, by testing the variant proteins in functional assays, addressing subcellular localization, and protein-protein interaction with the dimer partner PMS2 and the MMR-associated exonuclease 1. We show that a significant proportion of examined variant proteins have functional defects in either subcellular localization or protein-protein interactions, which is suspected to lead to the cancer phenotype observed in patients. Moreover, the obtained results correlate well with reported MMR activity and with in silico analysis for a majority of the variants.
Предметные рубрики MeSH
Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsColorectal Neoplasms, Hereditary NonpolyposisDNA Repair EnzymesDNA-Binding ProteinsEscherichia coli ProteinsHeLa CellsHumansMiceMismatch Repair Endonuclease PMS2Models, MolecularMutL Protein Homolog 1MutL ProteinsMutagenesis, Site-DirectedMutation, MissenseNIH 3T3 CellsNuclear ProteinsPolymorphism, Single NucleotideProtein BindingProtein Structure, TertiaryProtein TransportStructural Homology, Protein