Abstract
Death domain-associated protein (Daxx) was originally identii¬ed as a protein that specii¬cally binds to the death domain of the transmembrane death receptor Fas (also called CD95) in the cytoplasm and potentiates Fas-induced apoptosis. Over expression of Daxx enhances Fas-mediated apoptosis and activates the Jun N-terminal kinase (JNK) pathway. Daxx was found in the nuclears where it localizes to promyelocytic leukaemia (PML) oncogenic domains (PODs). As a highly conserved nuclear protein, Daxx plays an important role in proapoptosis, antiapoptosis and transcriptional regulation. This article reviews the latest advances in the study of the biological function of Daxx. Key words: Death domain-associated protein (Daxx), cell apoptosis, transcriptional regulation, biological function.
Highlights
Advances in the study of the biological function of DaxxDeath domain-associated protein (Daxx) was originally identified as a protein that binds to the death domain of the transmembrane death receptor Fas ( called CD95) in the cytoplasm and potentiates Fas-induced apoptosis
As a highly conserved nuclear protein, Death domainassociated protein (Daxx) was originally identified as a protein that binds to the death domain of the transmembrane, death receptor FAS in the cytoplasm and potentiates FAS-induced apoptosis (Yang et al, 1997)
We found out that over-expression of Daxx facilitated HepG2 cells apoptosis induced by hydrogen peroxide (Tuo et al, 2008)
Summary
Death domain-associated protein (Daxx) was originally identified as a protein that binds to the death domain of the transmembrane death receptor Fas ( called CD95) in the cytoplasm and potentiates Fas-induced apoptosis. Over expression of Daxx enhances Fas-mediated apoptosis and activates the Jun N-terminal kinase (JNK) pathway. Daxx was found in the nuclears where it localizes to promyelocytic leukaemia (PML) oncogenic domains (PODs). As a highly conserved nuclear protein, Daxx plays an important role in proapoptosis, antiapoptosis and transcriptional regulation. This article reviews the latest advances in the study of the biological function of Daxx
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