<i>Caenorhabditis elegans</i> DAF‐21 (HSP90) is characteristically and predominantly expressed in germline cells: Spatial and temporal analysis

Inoue, Tadao; Takamura, Kiyoko; Yamae, Hisanori; Ise, Naoto; Kawakami, Manabu; Tabuse, Yo; Miwa, Johji; Yamaguchi, Yasunori

doi:10.1046/j.1440-169x.2003.00706.x

Cited by 28 publications

(20 citation statements)

References 25 publications

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“…In C. elegans, all eggs are equally competent to hatch without any external stimulation (Albert and Riddle, 1988). The sensitivity of C. elegans egg hatch to GA exposure suggests the involvement of Hsp90 in this process, which is consistent with evidence for the presence of Hsp90/DAF-21 within the germline (Inoue et al, 2003). In contrast to C. elegans, the hatching process in cyst nematodes is complex, asynchronous, and influenced by environmental and host-derived factors (reviewed in Perry, 1997).…”

Section: Discussionsupporting

confidence: 75%

Effects of Geldanamycin on Hatching and Juvenile Motility in Caenorhabditis elegans and Heterodera glycines

Skantar¹,

Agama

Meyer³

et al. 2005

J Chem Ecol

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Abstract-Several Streptomyces species are known to produce metabolites that inhibit plant pathogens. One such compound is geldanamycin (GA), a benzoquinone ansamycin originally isolated from Streptomyces hygroscopicus. We examined the effect of geldanamycin on egg hatch and juvenile motility in Caenorhabditis elegans and in two populations of the plant-parasitic nematode Heterodera glycines. When C. elegans eggs were exposed to geldanamycin, both hatch and motility were reduced by GA doses between 2 and 50 mg/ml. The H. glycines inbred populations TN17 and TN18 exhibited low dose stimulation of hatch and motility, whereas levels occurring at higher GA doses were at or below control levels. These experiments represent the first demonstration of geldanamycin effects in C. elegans and H. glycines and suggest that the heat shock chaperone Hsp90, the known molecular target of geldanamycin, may be involved in nematode egg hatch and motility. This study also indicates that geldanamycin-producing strains of Streptomyces may be useful as biocontrol agents for nematodes.

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Section: Discussionsupporting

confidence: 75%

Effects of Geldanamycin on Hatching and Juvenile Motility in Caenorhabditis elegans and Heterodera glycines

Skantar¹,

Agama

Meyer³

et al. 2005

J Chem Ecol

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“…However, the apparent integrity of the pole plasm in Hsp83 stc /Hsp83 E317K ovaries and embryos (Figures 6 and 7) and the rescue of pgc localization upon overexpression of a single kinase (Figure 8) are consistent with the idea that the defects in pgc (and perhaps also nos) localization arise from the reduction in activity of a few discrete Hsp90 clients. Hsp83 mRNA is itself concentrated in the pole plasm (Ding et al 1993) and Hsp90 is found at particularly high levels in the germ line precursors of other organisms (Vanmuylder et al 2002;Inoue et al 2003), which may reflect a conserved role in mRNA localization.…”

Section: Discussionmentioning

confidence: 96%

The Molecular Chaperone Hsp90 Is Required for mRNA Localization in Drosophila melanogaster Embryos

et al. 2007

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Localization of maternal nanos mRNA to the posterior pole is essential for development of both the abdominal segments and primordial germ cells in the Drosophila embryo. Unlike maternal mRNAs such as bicoid and oskar that are localized by directed transport along microtubules, nanos is thought to be trapped as it swirls past the posterior pole during cytoplasmic streaming. Anchoring of nanos depends on integrity of the actin cytoskeleton and the pole plasm; other factors involved specifically in its localization have not been described to date. Here we use genetic approaches to show that the Hsp90 chaperone (encoded by Hsp83 in Drosophila) is a localization factor for two mRNAs, nanos and pgc. Other components of the pole plasm are localized normally when Hsp90 function is partially compromised, suggesting a specific role for the chaperone in localization of nanos and pgc mRNAs. Although the mechanism by which Hsp90 acts is unclear, we find that levels of the LKB1 kinase are reduced in Hsp83 mutant egg chambers and that localization of pgc (but not nos) is rescued upon overexpression of LKB1 in such mutants. These observations suggest that LKB1 is a primary Hsp90 target for pgc localization and that other Hsp90 partners mediate localization of nos.

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“…Before use, the EOR-1 antibody was preabsorbed with acetone powder made from eor-1(cs28) animals and diluted 1:2000. The anti-HSP90 antibody, a gift from Johji Miwa and Yasunori Yamaguchi, was previously described (Inoue et al 2003) and used at 1:1,000 to control for loading. The MEL-26 antibody, a gift from Paul Mains, was previously described (Pintard et al 2003) and used at 1:500.…”

Section: Methodsmentioning

confidence: 99%

EOR-2 Is an Obligate Binding Partner of the BTB–Zinc Finger Protein EOR-1 in Caenorhabditis elegans

et al. 2010

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BTB-zinc finger transcription factors play many important roles in metazoan development. In these proteins, the BTB domain is critical for dimerization and for recruiting cofactors to target genes. Identification of these cofactors is important for understanding how BTB-zinc finger proteins influence transcription. Here we show that the novel but conserved protein EOR-2 is an obligate binding partner of the BTB-zinc finger protein EOR-1 in Caenorhabditis elegans. EOR-1 and EOR-2 function together to promote multiple Ras/ERK-dependent cell fates during development, and we show that EOR-1 is a robust substrate of ERK in vitro. A point mutation (L81F) in the EOR-1 BTB domain reduces both ERK phosphorylation and EOR-2 binding and eliminates all detectable biological function without affecting EOR-1 expression levels, localization, or dimerization. This point mutation lies near the predicted charged pocket region of the EOR-1 BTB dimer, a region that, in other BTB-zinc finger proteins, has been proposed to interact with corepressors or coactivators. We also show that a conserved zinc finger-like motif in EOR-2 is required for binding to EOR-1, that the interaction between EOR-1 and EOR-2 is direct, and that EOR-2 can bind to the human BTB-zinc finger protein PLZF. We propose that EOR-2 defines a new family of cofactors for BTB-zinc finger transcription factors that may have conserved roles in other organisms.

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Caenorhabditis elegans DAF‐21 (HSP90) is characteristically and predominantly expressed in germline cells: Spatial and temporal analysis

Cited by 28 publications

References 25 publications

Effects of Geldanamycin on Hatching and Juvenile Motility in Caenorhabditis elegans and Heterodera glycines

Effects of Geldanamycin on Hatching and Juvenile Motility in Caenorhabditis elegans and Heterodera glycines

The Molecular Chaperone Hsp90 Is Required for mRNA Localization in Drosophila melanogaster Embryos

EOR-2 Is an Obligate Binding Partner of the BTB–Zinc Finger Protein EOR-1 in Caenorhabditis elegans

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