Abstract
Enzymes that covalently modify histones control many cellular processes by affecting gene expression. A new class of these enzymes is the histone lysine methyltransferase family, whose catalytic activity lies within a conserved domain, the SET domain. This article surveys the evidence for a connection between SET-domain-containing proteins and cancer. It proposes that deregulation of SET-domain function has an important role in carcinogenesis.
MeSH Terms
Amino Acid Sequence
Animals
Carrier Proteins/genetics,metabolism
DNA-Binding Proteins/genetics,metabolism
Histone Methyltransferases
Histone-Lysine N-Methyltransferase/genetics,metabolism
Humans
Intracellular Signaling Peptides and Proteins
Methyltransferases/genetics,metabolism
Mice
Molecular Sequence Data
Neoplasms/metabolism,physiopathology
Nuclear Proteins/genetics,metabolism
Protein Structure, Tertiary
Retinoblastoma Protein/metabolism
Saccharomyces cerevisiae Proteins/genetics,metabolism
Transcription Factors/genetics,metabolism
Chemicals
Carrier Proteins
DNA-Binding Proteins
Intracellular Signaling Peptides and Proteins
Nuclear Proteins
Retinoblastoma Protein
Saccharomyces cerevisiae Proteins
Transcription Factors
Histone Methyltransferases
Methyltransferases
SU(VAR)3-9
Set2 protein, S cerevisiae
Histone-Lysine N-Methyltransferase
NSD1 protein, human
Nsd1 protein, mouse
PRDM2 protein, human
SET1 protein, S cerevisiae
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Schneider Robert
Wellcome/Cancer Research UK Institute and Department of Pathology, Tennis Court Road, Cambridge, UK CB2 1QR.
Bannister Andrew J
Kouzarides Tony