Centrosome Biology: The Ins and Outs of Centrosome Assembly

Prosser, Suzanna L.; Pelletier, Laurence

doi:10.1016/j.cub.2015.06.038

Cited by 8 publications

(7 citation statements)

References 20 publications

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“…Because the adoption of Plk4's dot-like localization pattern is an obligatory step for triggering centriole biogenesis, Plk4's subcentrosomal localization and function are intricately regulated both by upstream scaffold proteins such as Cep192 and Cep152 and by subsequent events that modulate Plk4's LLPS activity. In recent years, multiple reviews have covered several areas, from identifying components for centriole assembly to PCM organization [20,[39][40][41]. Therefore, in light of the discovery that the novel Cep63-Cep152 self-assembly is critical for regulating Plk4 function, this review will focus on discussing: (i) the scaffold proteins instrumental for Plk4 recruitment and positioning in the subcentrosomal space, (ii) the structural features of the self-assembled Cep63-Cep152 architecture, and (iii) the physiological significance of the Cep63-Cep152 self-assembly in promoting Plk4-mediated centriole biogenesis.…”

Section: Centriole Biogenesis and The Role Of Inner Pericentriolar Mamentioning

confidence: 99%

A self-assembled cylindrical platform for Plk4-induced centriole biogenesis

et al. 2020

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The centrosome, a unique membraneless multiprotein organelle, plays a pivotal role in various cellular processes that are critical for promoting cell proliferation. Faulty assembly or organization of the centrosome results in abnormal cell division, which leads to various human disorders including cancer, microcephaly and ciliopathy. Recent studies have provided new insights into the stepwise self-assembly of two pericentriolar scaffold proteins, Cep63 and Cep152, into a near-micrometre-scale higher-order structure whose architectural properties could be crucial for proper execution of its biological function. The construction of the scaffold architecture appears to be centrally required for tight control of a Ser/Thr kinase called Plk4, a key regulator of centriole duplication, which occurs precisely once per cell cycle. In this review, we will discuss a new paradigm for understanding how pericentrosomal scaffolds are self-organized into a new functional entity and how, on the resulting structural platform, Plk4 undergoes physico-chemical conversion to trigger centriole biogenesis.

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Section: Centriole Biogenesis and The Role Of Inner Pericentriolar Mamentioning

confidence: 99%

A self-assembled cylindrical platform for Plk4-induced centriole biogenesis

et al. 2020

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“…Evidence suggests that they are heavily modified by post-translational modifications [6, 7] and thus are behaviorally distinct from spindle microtubules in terms of both inherent dynamics as well as resistance to commonly used cytotoxic drugs [8]. In contrast to centrioles, the surrounding PCM is structurally ill-defined and until recently has been described as an amorphous, proteinaceous matrix ([9]; for a more detailed review of PCM organization see [10]). The PCM serves as a recruiting center for several proteins [11] involved in the nucleation of microtubules, including the yTURC ring complex [12], and provides a structural scaffold to which newly nucleated microtubules can be anchored [13].…”

Section: Centrosome Structure and Functionmentioning

confidence: 99%

Centrosomal clustering contributes to chromosomal instability and cancer

Milunović-Jevtić

Mooney

Sulerud

et al. 2016

Current Opinion in Biotechnology

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Cells assemble mitotic spindles during each round of division to insure accurate segregation of their duplicated genome. In animal cells, stereotypical spindles have two poles, each containing one centrosome, from which microtubules are nucleated. In contrast, many cancer cells often contain more than two centrosomes and form transient multipolar spindle structures with more than two poles. In order to divide and produce viable progeny, the multipolar spindle intermediate must be reshaped into a pseudo-bipolar structure via a process called centrosomal clustering. Pseudo-bipolar spindles appear to function normally during mitosis, but they occasionally give rise to aneuploid and transformed daughter cells. Agents that inhibit centrosomal clustering might therefore work as a potential cancer therapy, specifically targeting mitosis in supernumerary centrosome-containing cells.

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“…One possibility is that a centrosome component is modified in mitotic cells and activates the interphase centrosome as the MTOC. The centrosome proteins SPD-2/Cep192 and SPD-5 recruit PCM and g-tubulin following phosphorylation by mitotic kinases, 4 but it is unknown how SPD-2 and SPD-5 themselves are recruited to the centrosome upon activation. To determine if the mitotic cell contributes these proteins to the interphase cell upon fusion, we marked the origin of proteins adding onto the centrosome in the interphase cell: GFP-tagged proteins were photobleached in a mitotic cell, which was then fused to an interphase cell.…”

Section: Flipping the Switch: Regulating Mtoc Locationmentioning

confidence: 99%

“…Consistent with this idea, recent reports show that centrosomal and cytoplasmic pools of SPD-2 exchange readily. 4,6 Future studies will reveal if CDKs directly modify SPD-2, if activated SPD-2 is sufficient to establish a centrosome MTOC, and how the membrane MTOC is switched off as the centrosome is switched on.…”

Section: Flipping the Switch: Regulating Mtoc Locationmentioning

confidence: 99%