CP110 Cooperates with Two Calcium-binding Proteins to Regulate Cytokinesis and Genome Stability

Tsang, William Y.W.; Spektor, Alexander; Luciano, Daniel; Indjeian, Vahan B.; Chen, Zhihong; Salisbury, Jeffery L.; Sánchez, Irma; Dynlacht, Brian David

doi:10.1091/mbc.e06-04-0371

Cited by 84 publications

(107 citation statements)

References 39 publications

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“…S8A,B,D,E) (Dobbelaere et al, 2008). CP110 in humans participates in other processes, such as preventing centrioles from nucleating cilia (Kleylein-Sohn et al, 2007;Spektor et al, 2007) and cytokinesis (Tsang et al, 2006). It has been proposed that centrioles might play an important role in signaling the event of cellular abscission in cytokinesis (Piel et al, 2001).…”

Section: Spd2 and Cp110 Emerged In A Taxon-specific Mannermentioning

confidence: 99%

Stepwise evolution of the centriole-assembly pathway

Carvalho-Santos

Machado

Branco

et al. 2010

Journal of Cell Science

205

278

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SummaryThe centriole and basal body (CBB) structure nucleates cilia and flagella, and is an essential component of the centrosome, underlying eukaryotic microtubule-based motility, cell division and polarity. In recent years, components of the CBB-assembly machinery have been identified, but little is known about their regulation and evolution. Given the diversity of cellular contexts encountered in eukaryotes, but the remarkable conservation of CBB morphology, we asked whether general mechanistic principles could explain CBB assembly. We analysed the distribution of each component of the human CBB-assembly machinery across eukaryotes as a strategy to generate testable hypotheses. We found an evolutionarily cohesive and ancestral module, which we term UNIMOD and is defined by three components (SAS6, SAS4/CPAP and BLD10/CEP135), that correlates with the occurrence of CBBs. Unexpectedly, other players (SAK/PLK4, SPD2/CEP192 and CP110) emerged in a taxon-specific manner. We report that gene duplication plays an important role in the evolution of CBB components and show that, in the case of BLD10/CEP135, this is a source of tissue specificity in CBB and flagella biogenesis. Moreover, we observe extreme protein divergence amongst CBB components and show experimentally that there is loss of cross-species complementation among SAK/PLK4 family members, suggesting species-specific adaptations in CBB assembly. We propose that the UNIMOD theory explains the conservation of CBB architecture and that taxon-and tissue-specific molecular innovations, gained through emergence, duplication and divergence, play important roles in coordinating CBB biogenesis and function in different cellular contexts. Journal of Cell ScienceTo investigate the existence of such a universal CBB-assembly mechanism, we searched for homologs of known CBB-assembly proteins in a set of 26 representative eukaryotic species, covering the crown eukaryotic groups and representing the diversity of function and architecture (including absence) of CBBs ( Fig. 2A,B; see supplementary material Tables S1 and S2). We calculated the correlation between the presence of each molecule and the presence of the CBB, using a normalized Hamming distance (Fig. 2). Given the poor annotation of the proteomes of certain species and the absence of structural information regarding the existence of a CBB in others, we arbitrarily defined that the presence of a molecule and the occurrence of the CBB structure were correlated if this occurred in at least 80% of the species (Fig. 2). To our surprise, given the conservation of the CBB structure, only a subset of CBBassembly proteins obey the criteria above defined: SAS4/CPAP, SAS6 and BLD10/CEP135 (Fig. 2). This evolutionarily cohesive behavior suggests that these three molecules are part of the same functional ancestral module in CBB assembly, which, for simplicity, we will call UNIversal MODule (UNIMOD). Amongst the six studied families, the UNIMOD components are, in fact, the only ones required to define the CBB architecture: SAS...

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Section: Spd2 and Cp110 Emerged In A Taxon-specific Mannermentioning

confidence: 99%

Stepwise evolution of the centriole-assembly pathway

Carvalho-Santos

Machado

Branco

et al. 2010

Journal of Cell Science

205

278

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“…An increasing number of centrosomal proteins have been reported to participate in cytokinesis, such as centriolin, Cep55, CP110 and BBS6 (Gromley et al, 2005;Fabbro et al, 2005;Tsang et al, 2006;Kim et al, 2005). Other major transitions where centrosome activity could impinge on the cell division cycle are the G1-S and G2-M transitions (Jackman et al, 2003;Mikule et al, 2007;Uetake et al, 2007) (for a review, see Doxsey et al, 2005).…”

Section: Centrosome Functionsmentioning

confidence: 99%

Structure and duplication of the centrosome

Azimzadeh

Bornens

2007

Journal of Cell Science

196

176

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“…29,30 Phosphorylation of one centrosomal protein named CP110 (centrosomal protein of 110 kDa) by multiple cyclin/Cdks, including cyclin A/Cdk2, is apparently critical for preventing premature centrosome separation and polyploidy that results from a cytokinesis failure. 31,32 Evidence has also pointed to a role for cyclin A in contributing to the microtubule nucleating activity of centrosomes, possibly at the onset of mitosis. 33 Furthermore, cyclin A, in concert with Cdk1, targets an unidentified cytoplasmic target to inhibit endocytic vesicle fusion.…”

Section: Cyclin a Localizationmentioning

confidence: 99%

“…It is possible, by virtue of the close proximity between the ER and the centrosome that SCAPER connects with the centrosomal protein CP110 via CaM, enabling its phosphorylation by cyclin A/Cdk2. To this end, it is interesting to note that CP110 is also a CaM-binding protein (Tsang et al, 2006). Furthermore, SCAPER is predicted to contain one putative transmembrane domain, suggesting that it may be a membrane-associated protein present at the ER.…”

Section: Scaper a New Cyclin A/cdk2-interacting Proteinmentioning

confidence: 99%

Double identity of SCAPER: A substrate and regulator of cyclin A/Cdk2

Tsang

Dynlacht²

2008

Cell Cycle

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Cyclin A is a key regulator of DNA replication and mitosis, and cyclin A/Cdk2 activity is critical for progression of cells from G 1 /S to M phase of the cell cycle. There is abundant evidence that cyclin A is predominantly localized to, and functions in, the nucleus, and a number of nuclear cyclin A/Cdk2 substrates have been identified. Evidence supporting the presence of cyclin A and its associated activity in the cytoplasm have also been reported, but the biological significance of this cyclin/Cdk pool during cell cycle progression remains controversial. Recently, we identified and characterized a new cyclin A/Cdk2 substrate named SCAPER which is localized to the endoplasmic reticulum. By sequestering cyclin A/Cdk2, SCAPER is capable of directing the activity of this kinase complex away from the nucleus and regulating cyclin A/Cdk2 equilibrium in distinct subcellular compartments. This work paves new avenues for understanding the role of cytoplasmic cyclin A/Cdk2 and its potential contribution to cancer and tumor formation.

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CP110 Cooperates with Two Calcium-binding Proteins to Regulate Cytokinesis and Genome Stability

Cited by 84 publications

References 39 publications

Stepwise evolution of the centriole-assembly pathway

Stepwise evolution of the centriole-assembly pathway

Structure and duplication of the centrosome

Double identity of SCAPER: A substrate and regulator of cyclin A/Cdk2

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