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Article

Disruption of protein-protein interaction hotspots in the C-terminal domain of MLH1 confers mismatch repair deficiency.

NAR cancer - 1 Dec 2025

Fishwick Keri M, Gomez Vieito Diego, Greco Giada, Collotta Giulio, Gatti Marco, Kulik Anastasija A, Guérois Raphaël, Corbeski Ivan, Phadte Ashutosh S, Senoussi Issam, Cejka Petr, Pluciennik Anna, Porro Antonio, Sartori Alessandro A

Abstract excerpt

MutLα, a heterodimer of MLH1 and PMS2, plays a key role in DNA mismatch repair (MMR), which maintains genomic stability by correcting replication errors. Loss of MLH1 function causes MMR deficiency (MMRd), leading to elevated mutation rates and increased cancer susceptibility. However, MMRd can offer a therapeutic advantage, as high tumour mutational burden enhances the efficacy of immune checkpoint inhibition....

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Topics

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Share to DNA Mismatch Repair
Share to Endodeoxyribonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Exodeoxyribonucleases

Share to Mismatch Repair Endonuclease PMS2

Share to Multifunctional Enzymes

Share to MutL Protein Homolog 1

Share to Neoplastic Syndromes, Hereditary

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 41480639
DOI: 10.1093/narcan/zcaf055
PMCID: PMC12754775

Genes

MLH1
PMS2
FAN1
MIP
EXO1
MSH3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of protein-protein interaction hotspots in the C-terminal domain of MLH1 confers mismatch repair deficiency.PMID 41480639Read ↗

Characterization of a highly conserved binding site of Mlh1 required for exonuclease I-dependent mismatch repair.Semantic proximity Read ↗

A conserved motif in the disordered linker of human MLH1 is vital for DNA mismatch repair and its function is diminished by a cancer family mutation.Semantic proximity Read ↗

Intrinsically disordered regions regulate both catalytic and non-catalytic activities of the MutLα mismatch repair complex.Semantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.Semantic proximity Read ↗

Identification of MLH2/hPMS1 dominant mutations that prevent DNA mismatch repair function.Semantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Mismatch repair MLH complexes make distinct contributions to post-replicative mismatch repair versus trinucleotide repeat expansionsSemantic proximity Read ↗

DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair.Semantic proximity Read ↗

FAN1-MLH1 interaction affects repair of DNA interstrand cross-links and slipped-CAG/CTG repeatsSemantic proximity Read ↗

Truncation of the C-terminus of human MLH1 blocks intracellular stabilization of PMS2 and disrupts DNA mismatch repair.Semantic proximity Read ↗

Identification of Lynch syndrome mutations in the MLH1-PMS2 interface that disturb dimerization and mismatch repair.Semantic proximity Read ↗

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