MEF2B C-terminal mutations enhance transcriptional activity and stability to drive B cell lymphomagenesis

Nat Commun. 2024 Aug 21;15(1):7195. doi: 10.1038/s41467-024-51644-8.

Abstract

The myocyte enhancer factor 2B (MEF2B) transcription factor is frequently mutated in germinal center (GC)-derived B-cell lymphomas. Its ammino (N)-terminal mutations drive lymphomagenesis by escaping interaction with transcriptional repressors, while the function of carboxy (C)-terminal mutations remains to be elucidated. Here, we show that MEF2B C-tail is physiologically phosphorylated at specific residues and phosphorylation at serine (S)324 is impaired by lymphoma-associated mutations. Lack of phosphorylation at S324 enhances the interaction of MEF2B with the SWI/SNF chromatin remodeling complex, leading to higher transcriptional activity. In addition, these mutants show an increased protein stability due to impaired interaction with the CUL3/KLHL12 ubiquitin complex. Mice expressing a phosphorylation-deficient lymphoma-associated MEF2B mutant display GC enlargement and develop GC-derived lymphomas, when crossed with Bcl2 transgenic mice. These results unveil converging mechanisms of action for a diverse spectrum of MEF2B mutations, all leading to its dysregulation and GC B-cell lymphomagenesis.

MeSH terms

  • Animals
  • B-Lymphocytes / metabolism
  • Cell Line, Tumor
  • Germinal Center / metabolism
  • HEK293 Cells
  • Humans
  • Lymphoma, B-Cell* / genetics
  • Lymphoma, B-Cell* / metabolism
  • Lymphoma, B-Cell* / pathology
  • MEF2 Transcription Factors* / genetics
  • MEF2 Transcription Factors* / metabolism
  • Mice
  • Mice, Transgenic
  • Mutation*
  • Phosphorylation
  • Protein Stability
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism

Substances

  • MEF2 Transcription Factors
  • MEF2B protein, human
  • Proto-Oncogene Proteins c-bcl-2