DNp63a , a critical pro-proliferative factor and a marker of epidermal stemness, associates with the Y-box binding protein 1 (YB-1), a member of the cold shock protein family. YB-1 is an oncogenic, nucleic acid binding protein with pleiotropic function. Mainly localized in the cytoplasm, YB-1 is involved in alternative splicing, regulation of transcription and translation. Here we show that DNp63a induces the accumulation of post-translationally modified forms of YB-1 in the nucleus.Sumoylation and ubiquitination are both involved in this phenomenon. Silencing of YB-1 in differentiating HaCaT kertinocytes induces cell cycle arrest. YB-1 knockdown cells show early decline of cyclin D1, increase of p21WAF and reduced expression of the envelop precursor protein, involucrin. In proliferating HaCaT and squamous carcinoma cells, YB-1 triggers cell detachment and apoptosis suggesting that the functional interaction between DNp63a and YB-1 cooperate to support survival and proliferation of basal and transformed keratinocytes.
DNp63a and YB1-dependent regulation of keratinocyte adhesion and survival / DI MARTINO, Orsola; Troiano, Annaelena; Schiano Lomoriello, Irene; DI GIROLAMO, Daniela; Vivo, Maria; di Iorio, Enzo; Pollice, Alessandra; LA MANTIA, Girolama; Calabro', Viola. - (2013). (Intervento presentato al convegno ABCD tenutosi a Ravenna nel settembre 2013).
DNp63a and YB1-dependent regulation of keratinocyte adhesion and survival
DI MARTINO, ORSOLA;TROIANO, ANNAELENA;DI GIROLAMO, DANIELA;VIVO, MARIA;POLLICE, ALESSANDRA;LA MANTIA, GIROLAMA;CALABRO', VIOLA
2013
Abstract
DNp63a , a critical pro-proliferative factor and a marker of epidermal stemness, associates with the Y-box binding protein 1 (YB-1), a member of the cold shock protein family. YB-1 is an oncogenic, nucleic acid binding protein with pleiotropic function. Mainly localized in the cytoplasm, YB-1 is involved in alternative splicing, regulation of transcription and translation. Here we show that DNp63a induces the accumulation of post-translationally modified forms of YB-1 in the nucleus.Sumoylation and ubiquitination are both involved in this phenomenon. Silencing of YB-1 in differentiating HaCaT kertinocytes induces cell cycle arrest. YB-1 knockdown cells show early decline of cyclin D1, increase of p21WAF and reduced expression of the envelop precursor protein, involucrin. In proliferating HaCaT and squamous carcinoma cells, YB-1 triggers cell detachment and apoptosis suggesting that the functional interaction between DNp63a and YB-1 cooperate to support survival and proliferation of basal and transformed keratinocytes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
