PerspectiveCell Biology

Puzzled by PML

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Science  26 Nov 2010:
Vol. 330, Issue 6008, pp. 1183-1184
DOI: 10.1126/science.1199405

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Promyelocytic leukemia (PML) protein nuclear bodies are one of many structures found in the nucleus of higher eukaryotes. There are about 10 to 30 of these spherical bodies per nucleus, ranging in size from ∼0.2 to 1 µm in diameter. PML nuclear bodies (also known as PML oncogenic domains, Kremer bodies, or nuclear dot 10s) are currently defined by the presence of the PML protein (1). They were first identified in the 1960s, but their relationship with PML protein was only described about 20 years ago (2, 3). PML protein inhibits cell cycle progression, promotes cell death, suppresses some types of oncogenic transformation and senescence, acts in stem cell renewal, and plays a role in defense against many viruses (15). Although these effects are well described, the underlying molecular mechanisms are not. On page 1247 of this issue, Giorgi et al. (6) propose that PML protein controls calcium signaling at the endoplasmic reticulum (ER), potentially increasing its functional diversity.