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Open AccessJournal ArticleDOI

The centrosome cycle: Centriole biogenesis, duplication and inherent asymmetries

Erich A. Nigg, +1 more
- 01 Oct 2011 - 
- Vol. 13, Iss: 10, pp 1154-1160
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TLDR
The spatial aspects of the centrosome duplication cycle, the mechanism of centriole assembly and the possible consequences of the inherent asymmetry of Centrosomes and centrosomes are discussed.
Abstract
Centrosomes are microtubule-organizing centres of animal cells. They influence the morphology of the microtubule cytoskeleton, function as the base for the primary cilium and serve as a nexus for important signalling pathways. At the core of a typical centrosome are two cylindrical microtubule-based structures termed centrioles, which recruit a matrix of associated pericentriolar material. Cells begin the cell cycle with exactly one centrosome, and the duplication of centrioles is constrained such that it occurs only once per cell cycle and at a specific site in the cell. As a result of this duplication mechanism, the two centrioles differ in age and maturity, and thus have different functions; for example, the older of the two centrioles can initiate the formation of a ciliary axoneme. We discuss spatial aspects of the centrosome duplication cycle, the mechanism of centriole assembly and the possible consequences of the inherent asymmetry of centrioles and centrosomes.

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Centrosome function and assembly in animal cells

TL;DR: Advances should ultimately allow the in vitro reconstitution of functional centrosomes from their component proteins to unlock the secrets of these enigmatic organelles.
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Subdiffraction-resolution fluorescence microscopy reveals a domain of the centrosome critical for pericentriolar material organization

TL;DR: It is demonstrated that the pericentriolar material is organized into two main structural domains: a layer juxtaposed to the centriole wall, and proteins extending farther away from the Centrosome organized in a matrix, using SIM and STORM subdiffraction-resolution microscopies.
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Targeting Mitosis in Cancer: Emerging Strategies

TL;DR: The concept of exploiting the genomic instability of tumor cells through therapeutic inhibition of mitotic checkpoints is discussed, and it is believed this strategy has a high likelihood of success given its potential to enhance therapeutic index by targeting tumor-specific vulnerabilities.
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Phase transitions and size scaling of membrane-less organelles.

TL;DR: The phase transitions that appear to govern the assembly of membrane-less cytoplasmic and nucleoplasmic structures exhibit an intrinsic dependence on cell size, and may explain the size scaling reported for a number of structures.
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Once and only once: mechanisms of centriole duplication and their deregulation in disease

TL;DR: A better understanding of the molecular mechanisms governing centriole biogenesis is understood, opening up new possibilities for targeting these pathways in the context of human disease.
References
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Journal ArticleDOI

The interphase microtubule aster is a determinant of asymmetric division orientation in Drosophila neuroblasts

TL;DR: The orientation of stem cell divisions is maintained beyond one cell cycle thanks to microtubule polymerization and apical centrosome positioning.
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Reappraisal of the Hansemann—Boveri hypothesis on the origin of tumors

TL;DR: The rare occurrence of a pluripolar spindle represented Boveri's paradigm for a type of abnormal mitosis that can produce a host of random chromosomal combinations.
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Protein phosphatase 2A-SUR-6/B55 regulates centriole duplication in C. elegans by controlling the levels of centriole assembly factors.

TL;DR: It is found that the PP2A catalytic subunit LET-92, the scaffolding subunit PAA-1, and the B55 regulatory subunit SUR-6 function together to positively regulate centriole assembly and promote centrioles assembly by protecting ZYG-1 and SAS-5 from degradation.
Journal ArticleDOI

Centriole maturation and transformation to basal body.

TL;DR: This review focuses on the formation of basal bodies in mammalian cells with an emphasis on basal bodies sprouting a primary cilium.
Journal ArticleDOI

Phosphorylation of SAS-6 by ZYG-1 Is Critical for Centriole Formation in C. elegans Embryos

TL;DR: It is demonstrated that the kinase ZYG-1 phosphorylates the coiled-coil protein SAS-6 at serine 123 in vitro and established that such phosphorylation ensures the maintenance of SAS-7 at the emerging centriole and thus for faithful cell division.
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