Knockdown of the centrosomal component SAS-5 results in defects in nuclear morphology in Caenorhabditis elegans

Schmutz, Cornelia; Spang, Anne

doi:10.1016/j.ejcb.2004.10.004

Cited by 6 publications

(4 citation statements)

References 20 publications

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“…The function of this attachment is unclear, but it can be speculated that these ER membranes also contain nuclear pore complex components. At least the MAN-1, a nuclear envelope marker [13] is localized at this stage in a manner indistinguishable from the ER markers HDEL-GFP or SP-12::GFP [11], [27] (Fig. 5).…”

Section: Discussionmentioning

confidence: 87%

N-Glycosylation Is Required for Secretion and Mitosis in C. elegans

Stevens

Spang

2013

PLoS ONE

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N-glycosylation of proteins is an essential process, and N-glucans serve as important beacons in protein folding and ER associated degradation. More importantly, N-glycosylation increases the structural repertoire of proteins because the addition of the N-glucan on proteins will serve as a base for further sugar additions in the Golgi apparatus, and hence complex three-dimensional structures can be build. N-glycosylation is mediated by the ER-resident OST complex, which is essential throughout eukaryotes. Partial knockdown of conserved OST complex members, such as C. elegans RIBO-1, led to an embryonic lethal phenotype. Although the ER morphology was not grossly altered in ribo-1(RNAi) oocytes and embryos, secretion of yolk and of the yolk receptor RME-2 was perturbed in those worms. Perhaps as a consequence of reduced arrival of N-glycosylated proteins at the plasma membrane, cytokinesis occurred less efficiently leading to multinuclear cells. Unexpectedly, we detected a chromosome segregation defect in ribo-1(RNAi) embryos suggesting an essential role of at least one N-glycosylated protein in metaphase-anaphase transition.

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Section: Discussionmentioning

confidence: 87%

N-Glycosylation Is Required for Secretion and Mitosis in C. elegans

Stevens

Spang

2013

PLoS ONE

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“…Seven C. elegans proteins have been shown to contribute to new centriole assembly. Four of these, SAS-4 (Kirkham et al, 2003;Leidel and Gönczy, 2003), SAS-5 (Dammermann et al, 2004;Delattre et al, 2004;Schmutz and Spang, 2005), SAS-6 (Dammermann et al, 2004;Leidel et al, 2005), and the atypical protein kinase ZYG-1 (O' Connell et al, 2001), localize to centrioles and are specifically required for centriole formation. Depletion of any of these proteins by RNAi results in specific failure of centrosome duplication.…”

Section: Centrosome Assembly and Duplicationmentioning

confidence: 99%

Cell division

Oegema¹

2006

WormBook

119

117

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The C. elegans embryo is a powerful model system for studying the mechanics of metazoan cell division. Its primary advantage is that the architecture of the syncytial gonad makes it possible to use RNAi to generate oocytes whose cytoplasm is reproducibly (typically >95%) depleted of targeted essential gene products via a process that does not depend exclusively on intrinsic protein turnover. The depleted oocytes can then be analyzed as they attempt their first mitotic division following fertilization. Here we outline the characteristics that contribute to the usefulness of the C. elegans embryo for cell division studies. We provide a timeline for the first embryonic mitosis and highlight some of its key features. We also summarize some of the recent discoveries made using this system, particularly in the areas of nuclear envelope assembly/dissassembly, centrosome dynamics, formation of the mitotic spindle, kinetochore assembly, chromosome segregation, and cytokinesis.

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“…TPXL‐1 has been shown to activate and target the Aurora kinase (AIR‐1) to microtubules, which is essential for mitotic spindle assembly [ 49 ], while GIP‐2 is a component of the γ‐tubulin ring complex needed for the nucleation of microtubules during mitotic spindle formation [ 50 ]. Faulty spindle organization is a common cause of embryonic lethality in C. elegans [ 58 , 59 ] and dysregulation of this process could explain the observed embryonic lethality in pph‐7 mutants. However, a potential role of PPH‐7 in spindle organization would need to be confirmed in further experiments.…”

Section: Discussionmentioning

confidence: 99%

The protein tyrosine phosphatase PPH‐7 is required for fertility and embryonic development in C. elegans at elevated temperatures

Franziscus,

Ritz,

Kappel

et al. 2024

FEBS Open Bio

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Post‐translational modifications are key in the regulation of activity, structure, localization, and stability of most proteins in eukaryotes. Phosphorylation is potentially the most studied post‐translational modification, also due to its reversibility and thereby the regulatory role this modification often plays. While most research attention was focused on kinases in the past, phosphatases remain understudied, most probably because the addition and presence of the modification is more easily studied than its removal and absence. Here, we report the identification of an uncharacterized protein tyrosine phosphatase PPH‐7 in C. elegans, a member of the evolutionary conserved PTPN family of phosphatases. Lack of PPH‐7 function led to reduction of fertility and embryonic lethality at elevated temperatures. Proteomics revealed changes in the regulation of targets of the von Hippel–Lindau (VHL) E3 ligase, suggesting a potential role for PPH‐7 in the regulation of VHL.

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Knockdown of the centrosomal component SAS-5 results in defects in nuclear morphology in Caenorhabditis elegans

Cited by 6 publications

References 20 publications

N-Glycosylation Is Required for Secretion and Mitosis in C. elegans

N-Glycosylation Is Required for Secretion and Mitosis in C. elegans

Cell division

The protein tyrosine phosphatase PPH‐7 is required for fertility and embryonic development in C. elegans at elevated temperatures

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