Histone deacetylase complex subunit SAP30-like (SAP30L)

Histone deacetylase complex subunit SAP30-like (SAP30L) is a nuclear protein that serves as a critical component of the Sin3A corepressor complex, which mediates histone deacetylation and chromatin remodeling. SAP30L enables DNA bending, histone and phosphatidylinositol phosphate binding, and zinc ion binding activities, functioning primarily in the negative regulation of transcription by RNA polymerase II. SAP30L acts as a scaffold bridging corepressor proteins to nucleosomes, directly interacting with core histones, DNA, and signaling phospholipids. Its DNA-binding and -bending function is mediated by a zinc-coordinating module, while redox-dependent modifications regulate its activity. SAP30L has a key role in recruitment of histone deacetylases to nucleosomes and thus in the organization of chromatin structure and transcriptional repression. In cancer, transcriptional repression of SAP30L, such as through long non-coding RNA (SAP30L-AS1), appears to promote tumor cell proliferation and suppress apoptosis, indicating a tumor-suppressive function in normal tissues.

Other names

SAP30LNS4ATP2Sin3-associated protein p30-likeSin3 corepressor complex subunit SAP30LHistone deacetylase complex subunit SAP30LFLJ11526HCV non-structural protein 4A-transactivated protein 2

Transcriptional repression via recruitment of Sin3A, HDAC1, HDAC2, histone binding, and chromatin remodeling. Regulation of chromatin accessibility through histone deacetylation (as part of the Sin3A-HDAC complex).