Journal of Glycomics & Lipidomics
Open Access

Abstract

A new protein interaction of the SETD1A methyltransferase complex: Linking epigenetic regulation to the DNA damage response

Manal Alsulami

SETD1A is a component of an histone methyltransferase assembly, analogous to the S. cerevisiae Set1/COMPASS complex. In mammalian cells, SET1/MLL histone methyltransferase (HMT) complexes methylate H3K4, resulting in an epigenetic mark generally associated with increased transcription. While the SET domain-containing proteins are believed to be non-redundant, the SET1/MLL complexes contain shared subunits such as WDR5 (WD repeat domain 5), RBBP5 (Retinoblastoma-binding protein 5), ASH2L (Absent, small or homeotic)-like), and HCF1 (host cell factor 1), as well as factors that may be unique to specific complex isoforms. Defects in SETD1A have been linked to a number of human diseases, including cancer and schizophrenia. It is the main catalytic component of a multiprotein complex that methylates lysine 4 of histone H3, a histone mark associated with gene activation. In humans, six related protein complexes with partly nonredundant cellular functions share several protein subunits but are distinguished by unique catalytic SET-domain proteins. To further investigate the role of SETD1A, we mapped the physical interactions of the protein under endogenous conditions in two cell lines (HEK and NT2).

Published Date: 2021-05-28; Received Date: 2020-11-05