Structure and duplication of the centrosome

Azimzadeh, Juliette; Bornens, Michel

doi:10.1242/jcs.005231

Cited by 196 publications

(180 citation statements)

References 52 publications

(42 reference statements)

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“…The failure of basal bodies to anchor could be explained by either a defect in centriole maturation or in centriolar satellite organization. Indeed, centriolar maturation is characterized by the acquisition of subdistal and distal appendages, which form the ciliary basal feet and transition fibres, respectively 34 . Both of them are required for cilia formation.…”

Section: Cyld Interacts With Cap350 At the Centrosome/basal Bodiesmentioning

confidence: 99%

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

et al. 2014

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CYLD is a tumour suppressor gene mutated in familial cylindromatosis, a genetic disorder leading to the development of skin appendage tumours. It encodes a deubiquitinating enzyme that removes Lys63-or linear-linked ubiquitin chains. CYLD was shown to regulate cell proliferation, cell survival and inflammatory responses, through various signalling pathways. Here we show that CYLD localizes at centrosomes and basal bodies via interaction with the centrosomal protein CAP350 and demonstrate that CYLD must be both at the centrosome and catalytically active to promote ciliogenesis independently of NF-kB. In transgenic mice engineered to mimic the smallest truncation found in cylindromatosis patients, CYLD interaction with CAP350 is lost disrupting CYLD centrosome localization, which results in cilia formation defects due to impairment of basal body migration and docking. These results point to an undiscovered regulation of ciliogenesis by Lys63 ubiquitination and provide new perspectives regarding CYLD function that should be considered in the context of cylindromatosis.

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Section: Cyld Interacts With Cap350 At the Centrosome/basal Bodiesmentioning

confidence: 99%

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

et al. 2014

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“…In this study, we describe the molecular characterization of Cep70 as a genuine centrosomal protein that localizes to the centrosome throughout the cell cycle. Cep70 thus joins the growing list of centrosomal proteins involved in the regulation of centrosome structure and function (10).…”

Section: Cep70 Plays a Significant Role In The Organization Of Both Pmentioning

confidence: 99%

“…The centrosome may also serve to regulate other fundamental cellular functions, such as cell polarity and motility (1). Much progress has been made in the past decade in the identification of novel centrosomal proteins (10,11), but their interplay with the well established centrosome/spindle pole-resident molecules, such as ␥-tubulin, to mediate the organization and assembly of the mitotic spindle remains elusive. In addition, the functional significance of proteins that reside in the centrosomal compartment is still a subject of intense research.…”

mentioning

confidence: 99%

CEP70 Protein Interacts with γ-Tubulin to Localize at the Centrosome and Is Critical for Mitotic Spindle Assembly

Shi

Sun

Liu

et al. 2011

Journal of Biological Chemistry

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Deregulation of the mitotic spindle has been implicated in genomic instability, an important aspect of tumorigenesis and malignant transformation. To ensure the fidelity of chromosome transmission, the mitotic spindle is assembled by exquisite mechanisms and orchestrated by centrosomes in animal cells. Centrosomal proteins especially are thought to act coordinately to ensure accurate spindle formation, but the molecular details remain to be investigated. In this study, we report the molecular characterization and functional analysis of a novel centrosomal protein, Cep70. Our data show that Cep70 localizes to the centrosome throughout the cell cycle and binds to the key centrosomal component, ␥-tubulin, through the peptide fragments that contain the coiled-coil domains. Our data further reveal that the centrosomal localization pattern of Cep70 is dependent on its interaction with ␥-tubulin. Strikingly, Cep70 plays a significant role in the organization of both preexisting and nascent microtubules in interphase cells. In addition, Cep70 is necessary for the organization and orientation of the bipolar spindle during mitosis. These results thus report for the first time the identification of Cep70 as an important centrosomal protein that interacts with ␥-tubulin and underscore its critical role in the regulation of mitotic spindle assembly.

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“…The centrosome, the primary microtubule-organizing centre of the cell, is comprised of two centrioles surrounded by pericentriolar material that nucleates microtubules [1]. Centrosome duplication is a highly regulated process whose accuracy is essential for genome integrity [2].…”

Section: Introductionmentioning

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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Structure and duplication of the centrosome

Cited by 196 publications

References 52 publications

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

CEP70 Protein Interacts with γ-Tubulin to Localize at the Centrosome and Is Critical for Mitotic Spindle Assembly

Tankyrase 1 regulates centrosome function by controlling CPAP stability

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