Stabilization of Cell Polarity by the C. elegans RING Protein PAR-2

Hao, Yingsong; Boyd, Lynn; Seydoux, Géraldine

doi:10.1016/j.devcel.2005.12.015

Cited by 140 publications

(195 citation statements)

References 39 publications

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“…PAR-2 contains a RING-finger domain, which has often been shown to function in E3 ubiquitin ligase complexes (Petroski and Deshaies 2005). Interestingly, this RING-finger domain was recently proposed to function in regulating PAR-2 protein levels in the embryo (Hao et al 2006). However, while the levels of PAR-2 are decreased in par-2(it5ts) embryos, we could not observe a detectable increase in PAR-2 levels in either rpn-10 mutants or rpn-10; par-2(it5ts) double mutants (data not shown).…”

Section: Discussionmentioning

confidence: 99%

A Genomewide Screen for Suppressors of par-2 Uncovers Potential Regulators of PAR Protein-Dependent Cell Polarity in Caenorhabditis elegans

Labbé

Pacquelet²,

Marty³

et al. 2006

Genetics

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The PAR proteins play an essential role in establishing and maintaining cell polarity. While their function is conserved across species, little is known about their regulators and effectors. Here we report the identification of 13 potential components of the C. elegans PAR polarity pathway, identified in an RNAi-based, systematic screen to find suppressors of par-2(it5ts) lethality. Most of these genes are conserved in other species. Phenotypic analysis of double-mutant animals revealed that some of the suppressors can suppress lethality associated with the strong loss-of-function allele par-2(lw32), indicating that they might impinge on the PAR pathway independently of the PAR-2 protein. One of these is the gene nos-3, which encodes a homolog of Drosophila Nanos. We find that nos-3 suppresses most of the phenotypes associated with loss of par-2 function, including early cell division defects and maternal-effect sterility. Strikingly, while PAR-1 activity was essential in nos-3; par-2 double mutants, its asymmetric localization at the posterior cortex was not restored, suggesting that the function of PAR-1 is independent of its cortical localization. Taken together, our results identify conserved components that regulate PAR protein function and also suggest a role for NOS-3 in PAR protein-dependent cell polarity.

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Section: Discussionmentioning

confidence: 99%

A Genomewide Screen for Suppressors of par-2 Uncovers Potential Regulators of PAR Protein-Dependent Cell Polarity in Caenorhabditis elegans

Labbé

Pacquelet²,

Marty³

et al. 2006

Genetics

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“…The pID3.01 vectors utilize the pie-1 59-and 39-UTR sequences to drive expression in the maternal germline (Pellettieri et al 2003;Hao et al 2006). Integrated transgenic strains were made by microparticle bombardment as described in Praitis et al (2001) to create the strain ZU32 {unc-119(ed3) III; czIs10[unc-119(1); pie-1TGFPTKSR-2a]}.…”

Section: Methodsmentioning

confidence: 99%

The Caenorhabditis elegans ekl (Enhancer of ksr-1 Lethality) Genes Include Putative Components of a Germline Small RNA Pathway

et al. 2008

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A canonical Ras-ERK signaling pathway specifies the fate of the excretory duct cell during Caenorhabditis elegans embryogenesis. The paralogs ksr-1 and ksr-2 encode scaffolding proteins that facilitate signaling through this pathway and that act redundantly to promote the excretory duct fate. In a genomewide RNAi screen for genes that, like ksr-2, are required in combination with ksr-1 for the excretory duct cell fate, we identified 16 ''ekl '' (enhancer of ksr-1 lethality) genes that are largely maternally required and that have molecular identities suggesting roles in transcriptional or post-transcriptional gene regulation. These include the Argonaute gene csr-1 and a specific subset of other genes implicated in endogenous small RNA processes, orthologs of multiple components of the NuA4/Tip60 histone acetyltransferase and CCR4/NOT deadenylase complexes, and conserved enzymes involved in ubiquitination and deubiquitination. The identification of four small RNA regulators (csr-1, drh-3, ego-1, and ekl-1) that share the Ekl phenotype suggests that these genes define a functional pathway required for the production and/or function of particular germline small RNA(s). These small RNAs and the other ekl genes likely control the expression of one or more regulators of Ras-ERK signaling that function at or near the level of kinase suppressor of Ras (KSR).

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“…PAR-2 prevents the return of the anterior PAR proteins to the posterior cortex by inhibiting a flow of cortical cytoplasm directed towards the posterior (Cheeks et al, 2004;Munro et al, 2004). In turn, phosphorylation by PKC-3 antagonizes the cortical localization of PAR-2, preventing the posterior PAR-2 domain from extending into the anterior (Hao et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

TheC. eleganshomolog ofDrosophilaLethal giant larvae functions redundantly with PAR-2 to maintain polarity in the early embryo

2010

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SUMMARYPolarity is essential for generating cell diversity. The one-cell C. elegans embryo serves as a model for studying the establishment and maintenance of polarity. In the early embryo, a myosin II-dependent contraction of the cortical meshwork asymmetrically distributes the highly conserved PDZ proteins PAR-3 and PAR-6, as well as an atypical protein kinase C (PKC-3), to the anterior. The RING-finger protein PAR-2 becomes enriched on the posterior cortex and prevents these three proteins from returning to the posterior. In addition to the PAR proteins, other proteins are required for polarity in many metazoans. One example is the conserved Drosophila tumor-suppressor protein Lethal giant larvae (Lgl). In Drosophila and mammals, Lgl contributes to the maintenance of cell polarity and plays a role in asymmetric cell division. We have found that the C. elegans homolog of Lgl, LGL-1, has a role in polarity but is not essential. It localizes asymmetrically to the posterior of the early embryo in a PKC-3-dependent manner, and functions redundantly with PAR-2 to maintain polarity. Furthermore, overexpression of LGL-1 is sufficient to rescue loss of PAR-2 function.LGL-1 negatively regulates the accumulation of myosin (NMY-2) on the posterior cortex, representing a possible mechanism by which LGL-1 might contribute to polarity maintenance.

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Stabilization of Cell Polarity by the C. elegans RING Protein PAR-2

Cited by 140 publications

References 39 publications

A Genomewide Screen for Suppressors of par-2 Uncovers Potential Regulators of PAR Protein-Dependent Cell Polarity in Caenorhabditis elegans

A Genomewide Screen for Suppressors of par-2 Uncovers Potential Regulators of PAR Protein-Dependent Cell Polarity in Caenorhabditis elegans

The Caenorhabditis elegans ekl (Enhancer of ksr-1 Lethality) Genes Include Putative Components of a Germline Small RNA Pathway

TheC. eleganshomolog ofDrosophilaLethal giant larvae functions redundantly with PAR-2 to maintain polarity in the early embryo

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