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