The mammalian interphase centrosome: two independent units maintained together by the dynamics of the microtubule cytoskeleton

Jean, Catherine; Tollon, Yvette; Raynaud-Messina, Brigitte; Wright, Michel

doi:10.1016/s0171-9335(99)80020-x

Cited by 37 publications

(48 citation statements)

References 52 publications

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“…Mitotic centrosomes were analysed using either GT335 or anti-centrin-2 antibodies. In cultures exposed to NOC, the overall centrosomal organization was altered in interphase cells, with centrosomes being typically distanced and displaced from the juxtanuclear region (data not shown), consistent with the established role of MTs in anchoring centrosomal structures to each other and to their subcellular site (Jean et al, 1999). Fig.…”

Section: Diplosome Splitting By Ranbp1 Requires Integrity Of Mitotic supporting

confidence: 75%

“…After duplication, centrosomes remain tethered together throughout most of interphase, then separate in late G2 and eventually migrate to form the spindle poles. MTs contribute to the link between centrosomes (Jean et al, 1999). Cohesion in G2 and separation in mitosis are also regulated by a network of specific factors (Meraldi and Nigg, 2001), including the centrosomal C-Nap1 protein (Mayor et al, 2000), its upstream kinase Nek2 (Meraldi and Nigg, 2001) and the Inh2 regulator of Nek2 (Eto et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Cohesion between parental centrioles requires MT integrity (Jean et al, 1999) and MT disruption by nocodazole favors the separation of parental centrosomes (Mayor et al, 2000). We wondered whether MTs are implicated in RanBP1-induced splitting between centrioles.…”

Section: Diplosome Splitting By Ranbp1 Requires Integrity Of Mitotic mentioning

confidence: 99%

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Mammalian RanBP1 regulates centrosome cohesion during mitosis

Fiore

Ciciarello

Mangiacasale

et al. 2003

Journal of Cell Science

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(2003). Mammalian RanBP1 regulates centrosome cohesion during mitosis. J. Cell Sci. 116, 3399-3411.The P values in Table 1 were incorrectly positioned in both the print and online versions of this paper. The corrected Table 1 is shown below. We apologise for any inconvenience caused. A, serum-starved (G0/G1) and restimulated cells harvested 9, 15 and 22 h after cell cycle entry. ErratumB, thymidine-arrested (G1/S) and released cells harvested 6, 7 and 8 h after S phase resumption.P values between vector and pRanBP1-transfected cultures were calculated using the χ 2 test; ns, not significant.

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Section: Diplosome Splitting By Ranbp1 Requires Integrity Of Mitotic supporting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

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Mammalian RanBP1 regulates centrosome cohesion during mitosis

Fiore

Ciciarello

Mangiacasale

et al. 2003

Journal of Cell Science

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“…Some ICA69, however, could still be detected on TGN38-labeled Golgi fragments scattered throughout the cells. Treatment of cells with nocodazole followed by taxol causes a redistribution and mild destabilization of the microtubule cytoskeleton similar to what occurs in the prophase of mitosis (18,49). In these conditions, ICA69 had a bipolar distribution that overlapped with TGN38 at opposite sides of the nucleus (Fig.…”

Section: Enrichment Of Ica69 On the Golgi Complex By Subcellularmentioning

confidence: 61%

Islet Cell Autoantigen of 69 kDa Is an Arfaptin-related Protein Associated with the Golgi Complex of Insulinoma INS-1 Cells

Spitzenberger

Pietropaolo

Verkade

et al. 2003

Journal of Biological Chemistry

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Islet cell autoantigen of 69 kDa (ICA69) is a cytosolic protein of still unknown function. Involvement of ICA69 in neurosecretion has been suggested by the impairment of acetylcholine release at neuromuscular junctions upon mutation of its homologue gene ric-19 in C. elegans. In this study, we have further investigated the localization of ICA69 in neurons and insulinoma INS-1 cells. ICA69 was enriched in the perinuclear region, whereas it did not co-localize with markers of synaptic vesicles/synaptic-like microvesicles. Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules. The association of ICA69 with these organelles was confirmed by immunoelectron microscopy. Virtually no ICA69 immunogold labeling was observed on secretory granules near the plasma membrane, suggesting that ICA69 dissociates from secretory granule membranes during their maturation. In silico sequence and structural analyses revealed that the N-terminal region of ICA69 is similar to the region of arfaptins that interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. ICA69 is therefore a novel arfaptin-related protein that is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.

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“…It is also this mature centriole that anchors the bulk of the MTs, whereas the other centriole is relatively free to move (Piel et al, 2000). The average distance between these two centrioles is variable, celltype dependent and influenced by cytoskeletal dynamics and physiological conditions (Buendia et al, 1990;Euteneuer and Schliwa, 1985;Holy et al, 1997;Jean et al, 1999;Rodionov and Borisy, 1997;Schliwa et al, 1983;Schliwa et al, 1982;Sherline and Mascardo, 1982).…”

Section: Introductionmentioning

confidence: 99%

Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion

Graser

Stierhof

Nigg

2007

Journal of Cell Science

186

226

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The centrosome duplicates during the cell cycle but functions as a single microtubule-organising centre until shortly before mitosis. This raises the question of how centrosome cohesion is maintained throughout interphase. One dynamic model proposes that parental centrioles are held together through centriole-associated, entangling filaments. Central to this model are C-Nap1, a putative centriolar docking protein and rootletin, a fibrous component. Here we identify two novel proteins, Cep68 and Cep215, as required for centrosome cohesion. Similar to rootletin, Cep68 decorates fibres emanating from the proximal ends of centrioles and dissociates from centrosomes during mitosis. Furthermore, Cep68 and rootletin depend both on each other and on C-Nap1 for centriole association. Unlike rootletin, overexpression of Cep68 does not induce extensive fibre formation, but Cep68 is readily recruited to ectopic rootletin fibres. These data suggest that Cep68 cooperates with rootletin and C-Nap1 in centrosome cohesion. By contrast, Cep215 associates with centrosomes throughout the cell cycle and does not appear to interact with Cep68, rootletin or C-Nap1. Instead, our data suggest that Cep215 functionally interacts with pericentrin, suggesting that both proteins influence centrosome cohesion through an indirect mechanism related to cytoskeletal dynamics.

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The mammalian interphase centrosome: two independent units maintained together by the dynamics of the microtubule cytoskeleton

Cited by 37 publications

References 52 publications

Mammalian RanBP1 regulates centrosome cohesion during mitosis

Mammalian RanBP1 regulates centrosome cohesion during mitosis

Islet Cell Autoantigen of 69 kDa Is an Arfaptin-related Protein Associated with the Golgi Complex of Insulinoma INS-1 Cells

Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion

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