Cell division

Oegema, Karen

doi:10.1895/wormbook.1.72.1

Cited by 119 publications

(122 citation statements)

References 70 publications

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“…As with yeast, we observed that none of the analyzed genes enhanced the lethality of the him-10(e1511ts)/NUF2 kinetochore component mutant ( Table 1), suggesting that the identified enhancers have a specific effect on the SAC pathway. The interaction data for mdf-1, mdf-2, and san-1 support previous findings that some synthetic interactions that are common to MAD1 and MAD2 are not shared by MAD3 ( Y54G9A.6/BUB3 enhances the lethality of SAC mutants: Next we tested a putative ortholog of the kinetochore-associated component Bub3, Y54G9A.6 (which we will refer to as bub-3; reviewed in Oegema and Hyman 2006;Stein et al 2007;Tarailo et al 2007), for genetic interaction with SAC mutants. bub-3(RNAi) animals do not display any obvious phenotypes ( Figure 2B); however, depletion of BUB-3 in the absence of MDF-1, MDF-2, or SAN-1 results in a significant decrease in viability, presumably due to elevated chromosome instability (Figure 2).…”

supporting

confidence: 76%

Synthetic Lethal Interactions Identify Phenotypic “Interologs” of the Spindle Assembly Checkpoint Components

Tarailo

Rose

2007

Genetics

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Here, we report genetic interactions with mdf-1(gk2)/MAD1 in Caenorhabditis elegans. Nine are evolutionarily conserved or phenotypic ''interologs'' and two are novel enhancers, hcp-1 and bub-3. We show that HCP-1 and HCP-2, the two CENP-F-related proteins, recently implicated in the spindle assembly checkpoint (SAC) function, do not have identical functions, since hcp-1(RNAi), but not hcp-2(RNAi), enhances the lethality of the SAC mutants.

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supporting

confidence: 76%

Synthetic Lethal Interactions Identify Phenotypic “Interologs” of the Spindle Assembly Checkpoint Components

Tarailo

Rose

2007

Genetics

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“…This pronuclear meeting occurs during centration and is also dependent on long microtubules and the dynein heavy chain subunit in C. elegans (DHC-1) (32,33). Therefore, if the genes specifically required for the centrosome centration anchor are inhibited, the meeting of the male and female pronuclei occurs, but the nucleus-centrosome complex does not reach the cell center.…”

Section: Resultsmentioning

confidence: 99%

Intracellular organelles mediate cytoplasmic pulling force for centrosome centration in the Caenorhabditis elegans early embryo

Kimura

2010

Proc. Natl. Acad. Sci. U.S.A.

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The centrosome is generally maintained at the center of the cell. In animal cells, centrosome centration is powered by the pulling force of microtubules, which is dependent on cytoplasmic dynein. However, it is unclear how dynein brings the centrosome to the cell center, i.e., which structure inside the cell functions as a substrate to anchor dynein. Here, we provide evidence that a population of dynein, which is located on intracellular organelles and is responsible for organelle transport toward the centrosome, generates the force required for centrosome centration in Caenorhabditis elegans embryos. By using the database of full-genome RNAi in C. elegans, we identified dyrb-1, a dynein light chain subunit, as a potential subunit involved in dynein anchoring for centrosome centration. DYRB-1 is required for organelle movement toward the minus end of the microtubules. The temporal correlation between centrosome centration and the net movement of organelle transport was found to be significant. Centrosome centration was impaired when Rab7 and RILP, which mediate the association between organelles and dynein in mammalian cells, were knocked down. These results indicate that minus end-directed transport of intracellular organelles along the microtubules is required for centrosome centration in C. elegans embryos. On the basis of this finding, we propose a model in which the reaction forces of organelle transport generated along microtubules act as a driving force that pulls the centrosomes toward the cell center. This is the first model, to our knowledge, providing a mechanical basis for cytoplasmic pulling force for centrosome centration.endosome | lysosome | pronuclear migration | the centrosome-organelle mutual pulling model | yolk granule

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“…We decided to use the C. elegans embryo as a model system because of its stereotypical first mitotic division. Analyzing the consequences of depleting essential chromosome components is also straight-forward in this system because RNAi can be used to generate oocytes reproducibly Ͼ95% depleted of targeted proteins that can be monitored as they progress through their first mitotic division after fertilization (22). During this division, mitotic prophase initiates when the oocyte and sperm-derived pronuclei are on opposite sides of the embryo and continues as the pronuclei migrate toward each other.…”

Section: Resultsmentioning

confidence: 99%

Molecular analysis of mitotic chromosome condensation using a quantitative time-resolved fluorescence microscopy assay

Maddox

Portier

Desai

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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111

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Chromosomes condense during mitotic entry to facilitate their segregation. Condensation is typically assayed in fixed preparations, limiting analysis of contributing factors. Here, we describe a quantitative method to monitor condensation kinetics in living cells expressing GFP fused to a core histone. We demonstrate the utility of this method by using it to analyze the molecular requirements for the condensation of holocentric chromosomes during the first division of the Caenorhabditis elegans embryo. In control embryos, the fluorescence intensity distribution for nuclear GFP:histone changes during two distinct time intervals separated by a plateau phase. During the first interval, primary condensation converts diffuse chromatin into discrete linear chromosomes. After the plateau, secondary condensation compacts the curvilinear chromosomes to form shorter bar-shaped structures. We quantitatively compared the consequences on this characteristic profile of depleting the condensin complex, the mitosis-specific histone H3 kinase Aurora B, the centromeric histone CENP-A, and CENP-C, a conserved protein required for kinetochore assembly. Both condensin and CENP-A play critical but distinct roles in primary condensation. In contrast, depletion of CENP-C slows but does not prevent primary condensation. Finally, Aurora B inhibition has no effect on primary condensation, but slightly delays secondary condensation. These results provide insights into the process of condensation, help resolve apparent contradictions from prior studies, and indicate that CENP-A chromatin has an intrinsic role in the condensation of holocentric chromosomes that is independent of its requirement for kinetochore assembly. Aurora B ͉ CENP-A ͉ condensin ͉ kinetochore ͉ C. elegans

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Cell division

Cited by 119 publications

References 70 publications

Synthetic Lethal Interactions Identify Phenotypic “Interologs” of the Spindle Assembly Checkpoint Components

Synthetic Lethal Interactions Identify Phenotypic “Interologs” of the Spindle Assembly Checkpoint Components

Intracellular organelles mediate cytoplasmic pulling force for centrosome centration in the Caenorhabditis elegans early embryo

Molecular analysis of mitotic chromosome condensation using a quantitative time-resolved fluorescence microscopy assay

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