SETD2 maintains nuclear lamina stability to safeguard the genome.

ABSTRACT: Histone methyltransferases play essential roles in the organization and function of chromatin. They are also frequently mutated in human diseases including cancer¹. One such often mutated methyltransferase, SETD2, associates co-transcriptionally with RNA polymerase II and catalyzes histone H3 lysine 36 trimethylation (H3K36me3) - a modification that contributes to gene transcription, splicing, and DNA repair². While studies on SETD2 have largely focused on the consequences of its catalytic activity, the non-catalytic functions of SETD2 are largely unknown. Here we report a catalysis-independent function of SETD2 in maintaining nuclear lamina stability and genome integrity. We found that SETD2, via its intrinsically disordered N-terminus, associates with nuclear lamina

SUBMITTER: Khan A 

PROVIDER: S-EPMC10557632 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature