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 family of chromatin modification proteins are involved in the regulation of cell cycle progression, apoptosis, and DNA repair. Members are found in yeast, animals and plants. They share significant sequence in their C-terminal regions containing PHD finger domains, which have been implicated in chromatin-mediated transcriptional regulation []. The family includes proteins YNG1, YNG2 and Pho23 from Saccharomyces cerevisiae [, ], png1 and png2 from Schizosaccharomyces pombe [], inhibitor of growth proteins ING1-5 from mammals [], and Arabidopsis homologues ING1 (At3g24010) and ING2 (At1g54390) [].
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 [, ].
