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Journal of Cell Science 116, e805-e805 (2003)
Copyright © 2003 The Company of Biologists Limited


In this issue

PARP-3: a marker for daughter centrioles


Poly (ADP-ribose) polymerases (PARPs) are enzymes that add ADP-ribose moieties to specific acceptor proteins. Best characterized are PARP-1 and PARP-2, which function as survival factors that modify nuclear proteins such as histones and topoisomerases during DNA damage signalling. Gilbert de Murcia and co-workers have now cloned and characterized a novel member of the PARP family, PARP-3, which might have a rather different function (see p. 1551). PARP-3 displays PARP activity in vitro, and its catalytic domain shares significant sequence similarity (61%) with PARP-1. The authors find that the protein localizes to centrosomes, where it associates with PARP-1. In contrast to PARP-1, however, PARP-3 is present only at daughter centrioles – and thus represents the first known marker protein for these structures. Murcia and co-workers show that overexpression of PARP-3 or its noncatalytic N-terminal domain causes cells to arrest at the G1/S transition of the cell cycle. This finding is particularly significant given recent work suggesting that centrosomes play a critical role in cell cycle progression. Moreover, since PARP-1 is also implicated, the enzymes might link DNA damage surveillance to a checkpoint controlling mitotic fidelity.


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Related articles in JCS:

PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression
Angélique Augustin, Catherine Spenlehauer, Hélène Dumond, Josiane Ménissier-de Murcia, Matthieu Piel, Anne-Catherine Schmit, Françoise Apiou, Jean-Luc Vonesch, Michael Kock, Michel Bornens, and Gilbert de Murcia
JCS 2003 116: 1551-1562. [Abstract] [Full Text]  




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