Control of nuclear centration in the <i>C. elegans</i> zygote by receptor-independent Gα signaling and myosin II

Goulding, Morgan Q; Canman, Julie C.; Senning, Eric N.; Marcus, Andrew H.; Bowerman, Bruce

doi:10.1083/jcb.200703159

Cited by 41 publications

(45 citation statements)

References 47 publications

(63 reference statements)

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“…elegans wild-type (N2), zen-4(or153) (Severson et al, 2000), goa-1(sa734) (Robatzek and Thomas, 2000), let-99(or204ts) (Goulding et al, 2007), as well as transgenic lines expressing GFP-NMY-2 and GFP-MOE (Motegi et al, 2006b;Munro et al, 2004) were maintained using standard protocols. The mutant strains were maintained at 16°C and shifted to 24°C for at least 24 hours prior to analysis.…”

Section: Nematodes and Rnaimentioning

confidence: 99%

Regulation of cortical contractility and spindle positioning by the protein phosphatase 6 PPH-6 in one-cell stageC. elegansembryos

et al. 2010

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There was an error published in Development 137, 237-247.In Fig. 2D, owing to the PPH-6 film being inadvertently flipped during scanning, the two lanes labelled as input instead showed flowthrough. A revised Fig. 2 with the correct input samples in D is shown below. In addition, a note has been added to the end of the legend to clarify the lack of GFP-SAPS-1 signal in these input lanes.This error does not affect the conclusions of this experiment or of the paper. The authors apologise to readers for this mistake. Western blot analysis using PPH-6 antibodies on wild-type or pph-6(RNAi) embryonic extracts. The blot was reprobed with α-tubulin antibodies as a loading control (bottom). Note the presence of two species, with the lower one exhibiting the predicted molecular weight of PPH-6 (∼37 kDa). Note also that the ratio between these two species varies among extracts (compare A with inputs in C). Similar variability is observed for SAPS-1 (B,C). The variation might be due to differences in the developmental stages of the embryos in the different preparations. (B) Western blot analysis of wild-type or saps-1(RNAi) embryonic extracts probed with SAPS-1 antibodies. Note presence of two major specific species, exhibiting the predicted molecular weight of the splice variants of SAPS-1 (∼80 kDa and 87 kDa). A non-specific band (NS) served as a loading control. (C) Coimmunoprecipitation from wild-type, pph-6(RNAi) or saps-1(RNAi) embryonic extracts using PPH-6 antibodies. Western blots were probed with antibodies against PPH-6, SAPS-1 or α-tubulin, as indicated. In the second row, the input is exposed 10 times longer than the IP. Input/IP=1:50. In three independent experiments, we observed that PPH-6 antibodies retrieved more PPH-6 from the saps-1(RNAi) extract than from the pph-6(RNAi) extract, despite similar depletion levels of PPH-6. Perhaps PPH-6 not bound to SAPS-1 is more accessible to PPH-6 antibodies. (D) Extract from embryos expressing GFP-SAPS-1 or from wild-type embryos immunoprecipitated with GFP antibodies and analyzed by western blot with GFP or PPH-6 antibodies, as indicated. Note that only the PPH-6 species with the lower molecular weight co-immunoprecipitates with GFP-SAPS-1. Input/IP=1:50 (overall levels of GFP-SAPS-1 protein in the embryonic lysates are low, hence the lack of detection of GFP-SAPS-1 in the input lanes). 2689

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Section: Nematodes and Rnaimentioning

confidence: 99%

Regulation of cortical contractility and spindle positioning by the protein phosphatase 6 PPH-6 in one-cell stageC. elegansembryos

et al. 2010

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“…The nucleus, which is the target of many signaling events, is also sensitive to contractility forces that affect its architecture, stiffness, localization within the cell and its activity, for instance with regard to chromatin remodeling, DNA synthesis and gene expression (Chang et al, 2013;Goulding et al, 2007;Guilluy et al, 2014;Hossain et al, 2006;Kim et al, 2005;Kiss et al, 2014;Maeda et al, 2013;SarasaRenedo et al, 2006;Song et al, 2002;Szabo et al, 2011). With these key regulatory roles, it is not surprising that contractility has been shown to affect cell proliferation and differentiation in several experimental systems (Chowdhury et al, 2010;Ozdemir et al, 2013;Rottmar et al, 2014).…”

Section: Cellular Functions Of the Contractomementioning

confidence: 99%

The contractome – a systems view of actomyosin contractility in non-muscle cells

Zaidel-Bar

Guo

Luxenburg

2015

Journal of Cell Science

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Actomyosin contractility is a highly regulated process that affects many fundamental biological processes in each and every cell in our body. In this Cell Science at a Glance article and the accompanying poster, we mined the literature and databases to map the contractome of non-muscle cells. Actomyosin contractility is involved in at least 49 distinct cellular functions that range from providing cell architecture to signal transduction and nuclear activity. Containing over 100 scaffolding and regulatory proteins, the contractome forms a highly complex network with more than 230 direct interactions between its components, 86 of them involving phosphorylation. Mapping these interactions, we identify the key regulatory pathways involved in the assembly of actomyosin structures and in activating myosin to produce contractile forces within non-muscle cells at the exact time and place necessary for cellular function.

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“…2 and 3). However, a growing list of actin-dependent nuclear movements have been described including the movement of root tip nuclei during root growth in Arabidopsis, 7 axial expansion of nuclei in the Drosophila melanogastar syncytial blastoderm, 8 nuclear centration in the Caenorhabditis elegans zygote, 9 and rearward movement of nuclei to orient the centrosome for migration in fibroblasts 10 ( Table 1). Interestingly, there are types of nuclear movement which use forces generated by both microtubules and actin, such as nucleokinesis during neuronal cell migration [11][12][13] and interkinetic nuclear …”

mentioning

confidence: 99%

TAN lines

Luxton

Gomes

Folker

et al. 2011

Nucleus

112

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N uclear position is actively controlled and can be adjusted according to the needs of a cell by nuclear movement. Microtubules mediate the majority of nuclear movements studied to date, although examples of nuclear movements mediated by the actin cytoskeleton have been described. One such actin-dependent nuclear movement occurs during centrosome orientation in fibroblasts polarizing for migration. Here, the centrosome is maintained at the cell center while the nucleus is moved to the cell rear by actin retrograde flow thus positioning the centrosome between the nucleus and the leading edge of the cell. We have explored the molecular mechanism for actin dependent movement of the nucleus during centrosome orientation. We found that a novel linear array of nuclear envelope membrane proteins composed of nesprin-2G and SUN2, called transmembrane actin-associated nuclear (TAN) lines, couple the nucleus to moving actin cables resulting in the nucleus being positioned at the cell rear. TAN lines are anchored by A-type lamins and this allows the forces generated by the actin cytoskeleton to be transmitted across the nuclear envelope to move the nucleus. Here we review the data supporting this mechanism for nuclear movement, discuss questions remaining to be addressed and consider how this new mechanism of nuclear movement may shed light on human disease.

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Control of nuclear centration in the C. elegans zygote by receptor-independent Gα signaling and myosin II

Cited by 41 publications

References 47 publications

Regulation of cortical contractility and spindle positioning by the protein phosphatase 6 PPH-6 in one-cell stageC. elegansembryos

Regulation of cortical contractility and spindle positioning by the protein phosphatase 6 PPH-6 in one-cell stageC. elegansembryos

The contractome – a systems view of actomyosin contractility in non-muscle cells

TAN lines

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