Geminin cleavage during apoptosis by caspase-3 alters its binding ability to the SWI/SNF subunit Brahma.
作者： Vassilis Roukos , Maria S. Iliou , Hideo Nishitani , Marc Gentzel , Matthias Wilm
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摘要: Geminin has been proposed to coordinate cell cycle and differentiation events through balanced interactions with the regulator Cdt1 homeobox transcription factors chromatin remodeling activities implicated in fate decisions. Here we show that is cleaved primary cells cancer lines induced undergo apoptosis by a variety of stimuli. targeting mediated caspase-3 both vivo vitro. Two sites at carboxyl terminus (named C1 C2) are caspase, producing truncated forms Geminin. We provide evidence cleavage regulated phosphorylation. Casein kinase II alters site vitro, whereas mutating phosphorylation competent Ser/Thr residues proximal affects vivo. produced can promote apoptosis. In contrast, C2 lost ability interact Brahma (Brm), catalytic subunit SWI/SNF complex, while binding efficiently Cdt1, indicating during differentially its partners.
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