PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression

Augustin, Angélique; Spenlehauer, Catherine; Dumond, Hélène; Murcia, Josiane Ménissier‐de; Piel, Matthieu; Schmit, Anne‐Catherine; Apiou, Françoise; Vonesch, Jean‐Luc; Kock, Michael D.; Bornens, Michel; Murcia, Gilbert de

doi:10.1242/jcs.00341

Cited by 136 publications

(125 citation statements)

References 53 publications

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“…At least two other centrosomal proteins Cep76 [22] and Cep170 [23] contain RXXPDG TNKS1 binding sites and a number of other centrosomal proteins contain degenerate motifs, raising the possibility that TNKS could regulate stability of additional centrosomal proteins. Previous studies have demonstrated localization of other PARPs (PARP1 [24] and PARP3 [25]) to interphase centrosomes and PARP1 was found to be required for maintenance of proper centrosome number [26]. Hence, PARsylation (through multiple PARPs and targets) may have a general role in centrosome function.…”

Section: Resultsmentioning

confidence: 99%

Tankyrase 1 regulates centrosome function by controlling CPAP stability

2012

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CPAP-a gene mutated in primary microcephaly-is required for procentriole formation. Here we show that CPAP degradation and function is controlled by the poly(ADP-ribose) polymerase tankyrase 1. CPAP is PARsylated by tankyrase 1 in vitro and in vivo. Overexpression of tankyrase 1 leads to CPAP proteasomal degradation, preventing centriole duplication, whereas depletion of tankyrase 1 stabilizes CPAP in G1, generating elongated procentrioles and multipolarity. Tankyrase 1 localizes to centrosomes exclusively in G1, coinciding with CPAP degradation. Hence, tankyrase 1-mediated PARsylation regulates CPAP levels during the cell cycle to limit centriole elongation and ensure normal centrosome function.

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Section: Resultsmentioning

confidence: 99%

Tankyrase 1 regulates centrosome function by controlling CPAP stability

2012

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“…The third member of the DNA-dependent PARPs, PARP-3, is similar to PARP-1 and PARP-2 except that it is missing a known DNAbinding domain (Johansson, 1999). PARP-3 has been shown to associate with the centrosome, polycomb group proteins, and DNA repair machinery (Augustin et al, 2003;Rouleau et al, 2007). A recent study in astrocytes suggests that all three DNA-dependent PARPs can act cooperatively during activation of this cell type (Phulwani and Kielian, 2008).…”

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confidence: 99%

The Paralogous GenesRADICAL-INDUCED CELL DEATH1andSIMILAR TO RCD ONE1Have Partially Redundant Functions during Arabidopsis Development

2009

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RADICAL-INDUCED CELL DEATH1 (RCD1) and SIMILAR TO RCD ONE1 (SRO1) are the only two proteins encoded in the Arabidopsis (Arabidopsis thaliana) genome containing both a putative poly(ADP-ribose) polymerase catalytic domain and a WWE protein-protein interaction domain, although similar proteins have been found in other eukaryotes. Poly(ADP-ribose) polymerases mediate the attachment of ADP-ribose units from donor NAD + molecules to target proteins and have been implicated in a number of processes, including DNA repair, apoptosis, transcription, and chromatin remodeling. We have isolated mutants in both RCD1 and SRO1, rcd1-3 and sro1-1, respectively. rcd1-3 plants display phenotypic defects as reported for previously isolated alleles, most notably reduced stature. In addition, rcd1-3 mutants display a number of additional developmental defects in root architecture and maintenance of reproductive development. While single mutant sro1-1 plants are relatively normal, loss of a single dose of SRO1 in the rcd1-3 background increases the severity of several developmental defects, implying that these genes do share some functions. However, rcd1-3 and sro1-1 mutants behave differently in several developmental events and abiotic stress responses, suggesting that they also have distinct functions. Remarkably, rcd1-3; sro1-1 double mutants display severe defects in embryogenesis and postembryonic development. This study shows that RCD1 and SRO1 are at least partially redundant and that they are essential genes for plant development.

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“…Thus, CSPP could interact with proteins involved in centrosome maturation in G 1 and overexpression might lead to sequestration of binding partners and hence to centrosome dysfunction. Potential binding partners for CSPP could be PCM-1, PARP-3, centriolin, NPM/B23 or dynactin subunits, all of which have been shown to be involved in centrosome maturation/recruitment of cellcycle regulators at the G 1 /S-phase transition (Okuda et al, 2000;Balczon et al, 2002;Quintyne and Schroer, 2002;Augustin et al, 2003;Gromley et al, 2003). The effects of ectopic overexpression should be interpreted carefully since it may affect the activity and level of endogenous CSPP that again might be normally regulated at the level of phosphorylation.…”

Section: Discussionmentioning

confidence: 99%

Identification of a novel centrosome/microtubule-associated coiled-coil protein involved in cell-cycle progression and spindle organization

et al. 2004

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Here we describe the identification of a novel vertebratespecific centrosome/spindle pole-associated protein (CSPP) involved in cell-cycle regulation. The protein is predicted to have a tripartite domain structure, where the N-and C-terminal domains are linked through a coiledcoil mid-domain. Experimental analysis of the identified domains revealed that spindle association is dependent on the N-terminal and the coiled-coil mid domain. The expression of CSPP at the mRNA level was detected in all tested cell lines and in testis tissue. Ectopic expression of CSPP in HEK293T cells blocked cell-cycle progression in early G 1 phase and in mitosis in a dose-dependent manner. Interestingly, mitosis-arrested cells contained aberrant spindles and showed impairment of chromosome congression. Inhibition of CSPP gene expression by small interfering RNAs induced cell-cycle arrest/delay in S phase. This phenotype was characterized by elevated levels of cyclin A, decreased levels of cyclin E and hyperphosphorylation of the S-phase checkpoint kinase Chk1. The activation of Chk1 may indicate a replication stress response due to an inappropriate G 1 /S-phase transition. Taken together, we demonstrate that CSPP is associated with centrosomes and microtubules and may play a role in the regulation of G 1 /S-phase progression and spindle assembly.

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PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression

Cited by 136 publications

References 53 publications

Tankyrase 1 regulates centrosome function by controlling CPAP stability

Tankyrase 1 regulates centrosome function by controlling CPAP stability

The Paralogous GenesRADICAL-INDUCED CELL DEATH1andSIMILAR TO RCD ONE1Have Partially Redundant Functions during Arabidopsis Development

Identification of a novel centrosome/microtubule-associated coiled-coil protein involved in cell-cycle progression and spindle organization

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