IMR Press / FBL / Volume 13 / Issue 18 / DOI: 10.2741/3216

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
PML NBs (ND10) and Daxx: from nuclear structure to protein function
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1 Department of Anatomy and Cell Biology & Shands Cancer Center, University of Florida College of Medicine, 1376 Mowry Road, Gainesville FL 32610, USA

*Author to whom correspondence should be addressed.

Academic Editor: Katherine Borden

Front. Biosci. (Landmark Ed) 2008, 13(18), 7132–7142; https://doi.org/10.2741/3216
Published: 1 May 2008
Abstract

Proteins that combine PML NBs (ND10) can be divided into two groups: "transient" (that accumulate at PML NBs upon over-expression, interferon-induced up-regulation, block of proteosomal degradation, environmental stress or viral infection) and "constitutive" that co-localize with PML in the majority of cultured cells. One of the few "constitutive" components of PML NBs is the death domain-associated protein Daxx. While PML NBs are the most obvious depositories of Daxx, there are multiple alternative localization of this protein in the nucleus and cytoplasm, suggesting differential functionality of Daxx at different cellular compartments and stages of the cell cycle. The purpose of this review is to analyze Daxx spatiotemporal behavior within and outside of PML NBs and to discuss functions attributed to these localizations. We suggest that Daxx can participate in numerous cellular functions as a mediator of protein interactions, thus acting as a fine tuning instrument in highly orchestrated cellular processes; we also envision PML NBs accumulation of Daxx as an "out of action" storage depot.

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