Unknown

Dataset Information

0

SETting the Stage for Cancer Development: SETD2 and the Consequences of Lost Methylation.


ABSTRACT: The H3 lysine 36 histone methyltransferase SETD2 is mutated across a range of human cancers. Although other enzymes can mediate mono- and dimethylation, SETD2 is the exclusive trimethylase. SETD2 associates with the phosphorylated carboxy-terminal domain of RNA polymerase and modifies histones at actively transcribed genes. The functions associated with SETD2 are mediated through multiple effector proteins that bind trimethylated H3K36. These effectors directly mediate multiple chromatin-regulated processes, including RNA splicing, DNA damage repair, and DNA methylation. Although alterations in each of these processes have been associated with SETD2 loss, the relative role of each in the development of cancer is not fully understood. Critical vulnerabilities resulting from SETD2 loss may offer a strategy for potential therapeutics.

SUBMITTER: Fahey CC 

PROVIDER: S-EPMC5411680 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

SETting the Stage for Cancer Development: SETD2 and the Consequences of Lost Methylation.

Fahey Catherine C CC   Davis Ian J IJ  

Cold Spring Harbor perspectives in medicine 20170501 5


The H3 lysine 36 histone methyltransferase <i>SETD2</i> is mutated across a range of human cancers. Although other enzymes can mediate mono- and dimethylation, SETD2 is the exclusive trimethylase. SETD2 associates with the phosphorylated carboxy-terminal domain of RNA polymerase and modifies histones at actively transcribed genes. The functions associated with SETD2 are mediated through multiple effector proteins that bind trimethylated H3K36. These effectors directly mediate multiple chromatin-  ...[more]

Similar Datasets

| S-EPMC1299289 | biostudies-literature
| S-EPMC8294582 | biostudies-literature
| S-EPMC10268010 | biostudies-literature
| S-EPMC7902933 | biostudies-literature
| S-EPMC4811507 | biostudies-literature
| S-EPMC3716680 | biostudies-literature
| S-EPMC5770597 | biostudies-literature
| S-EPMC9102808 | biostudies-literature
| S-EPMC6642692 | biostudies-literature
| S-EPMC2168397 | biostudies-literature