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Signal transduction

Marked for nuclear export?

Nature volume 394, pages 619–620 (1998)Cite this article

The nucleus of a eukaryotic cell contains all the information needed for that cell to proliferate, differentiate or undergo programmed death (apoptosis). Which of these programmes is followed depends on signals sent to the nucleus in response to external cues such as growth factors. These bind to receptors at the plasma membrane and transduce signals to the inside through the generation of second messengers. On page 697 of this issue, Topham et al.1 present a new twist to one of the mechanisms by which this occurs.

Signal transduction into the nucleus can occur through the generation of diacylglycerol (DAG), a membrane-bound second messenger that activates protein kinase C (PKC)2. Upon growth-factor stimulation, PKC can translocate into the nucleus3 and phosphorylate a number of nuclear targets (such as the nuclear lamins4). Herein lies the problem. Some isoforms of PKC are absolutely dependent on DAG and, as this lipid is unlikely to translocate with the kinase, how are the levels of DAG in the nucleus coordinated with the presence of nuclear PKC? Topham and co-workers suggest that PKC can, itself, regulate the levels of nuclear DAG by inhibiting the nuclear entry of DAG kinase ζ (DGK-ζ), an enzyme that removes DAG. Furthermore, by genetically manipulating the levels of DAG kinase, the authors show that nuclear DAG is essential in regulating the cell cycle.

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Figure 1: Possible mechanisms for the regulation of nuclear diacylglycerol (DAG), based on the results of Topham et al.1 and others.

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  1. the Department of Cellular Biochemistry, The Netherlands Cancer Institute, Plesmanlaan 121, 1066cx, Amsterdam, The Netherlands

    Nullin Divecha

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  1. Nullin Divecha
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Divecha, N. Marked for nuclear export?. Nature 394, 619–620 (1998). https://doi.org/10.1038/29174

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