Sin3a is a transcriptional repressor and a homologue of the SIN3 repressor from yeast. Sin3a associates with the strong repressive isoform of Mxi1, a helix-loop-helix leucone zipper that associates with Max to antagonize Myc oncogenic activities []. Unlike Mxi1 and Myc, expression of Sin3a does not vary during development []. Sin3a is a component of several complexes, including the REST-CoREST repressor complex [], the PER complex which maintains circadian rhythm []and the Sin3 HDAC complex []. Sin3a also interacts with FOXK1 to regulate cell cycle progression []. Sin3a has three PAH domains by which it interacts with HCFC1, REST and SAP30 [, ].
This entry represents a domain found in the C-terminal of the transcriptional repressor Sin3.Budding yeast Sin3 is a component of both the Rpd3S and Rpd3L histone deacetylase complexes []. In mammals there are two Sin3 paraologues, Sin3A and Sin3B. They forms the larger Sin3L/Rpd3L and the smaller Sin3S/Rpd3S complexes, both complexes rely largely on HDAC (histone deacetylase) activity to affect transcriptional repression. Sin3A and Sin3B may partition into the Sin3L/Rpd3L and Sin3S/Rpd3S complexes, respectively [].
This domain is found in the transcriptional repressor Sin3. It forms interactions with histone deacetylases [].Budding yeast Sin3 is a component of both the Rpd3S and Rpd3L histone deacetylase complexes []. In mammals there are two Sin3 paraologues, Sin3A and Sin3B. They forms the larger Sin3L/Rpd3L and the smaller Sin3S/Rpd3S complexes, both complexes rely largely on HDAC (histone deacetylase) activity to affect transcriptional repression. Sin3A and Sin3B may partition into the Sin3L/Rpd3L and Sin3S/Rpd3S complexes, respectively [].
AT-rich interactive domain-containing protein 4B (ARID4B) acts as a transcriptional repressor. It may function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes []. It may play an integral part in the AR (androgen receptor) and RB (retinoblastoma) regulatory pathways involved in the regulation of Sertoli cell function and male fertility []. It is linked to tumor growth and metastasis [].
Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors isregulated by enzymes that acetylate and deacetylate histones. The Sin3A-histone deacetylase (HDAC) co-repressor complex consists of multiple proteins and regulates gene expression by deacetylating histones.This entry includes both Sin3-associated protein 30 (SAP30) and SAP30L, a close homologue of SAP30. Both are able to target Sin3A to the nucleolus [].
Members of the ING (inhibitor of growth protein) family of tumour suppressors regulate cell cycle progression, senescence, apoptosis, and DNA repair as important cofactors of p53. Inhibitorof growth protein 2 (ING2) seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53 []. It is also a component of a chromatin-modifying complex containing the transcriptional co-repressor SIN3A and HDAC1 (histone deacetylase 1), which is involved in deacetylation of nucleosomal histones [, ]. The stability of ING2 is regulated by nuclear phosphatidylinositol-5-phosphate at discrete chromatin targets in response to DNA damage [, ].
This entry represents the PHD domain of ING2.Members of the ING (inhibitor of growth protein) family of tumour suppressors regulate cell cycle progression, senescence, apoptosis, and DNA repair as important cofactors of p53. Inhibitor of growth protein 2 (ING2) seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53 []. It is also a component of a chromatin-modifying complex containing the transcriptional co-repressor SIN3A and HDAC1 (histone deacetylase 1), which is involved in deacetylation of nucleosomal histones [, ]. The stability of ING2 is regulated by nuclear phosphatidylinositol-5-phosphate at discrete chromatin targets in response to DNA damage [, ].
