This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and the cytoplasm.

Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli.

The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination.

Some kind of positive feedback system was also discovered; JNK activates HIPK2, which stands for the translocation of nuclear Daxx to the cytoplasm.

TGF-β regulates a variety of different cellular developmental processes including growth, differentiation, proliferation, and cell death.

Daxx interacts with the TGF-β type II receptor by binding of C-terminal domain of the protein.

Glucose breakdown produces ROS, which leads to Daxx production and relocalization, activating JNK pathway in turn.

Other studies showed that lack of Daxx gene caused a higher apoptotic rate in embryonic stem cells.

The omnipresence of Daxx in the cell nucleus suggests that the protein may also function as a transcription factor.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.