Transgene‐coded chimeric proteins as reporters of intracellular proteolysis: Starvation‐induced catabolism of a lacZ fusion protein in muscle cells of Caenorhabditis elegans

Zdinak, Lisa A.; Greenberg, I.; Szewczyk, Nathaniel J.; Barmada, Sami J.; Cardamone-Rayner, Mark; Hartman, James J.; Jacobson, Lewis A.

doi:10.1002/(sici)1097-4644(19971001)67:1<143::aid-jcb15>3.3.co;2-f

Cited by 14 publications

(54 citation statements)

References 31 publications

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“…This is consistent with reports that proteolysis in C. elegans muscle is repressed under basal conditions (i.e., in well-fed animals without deficits in insulin signaling pathways). 64,65 Therefore, we conclude that Aβ-induced autophagosome accumulation in muscle is the result of not only impaired but also upregulated autophagic activity (see Fig. 10).…”

Section: Do Not Distributementioning

confidence: 78%

Decreased Insulin-Receptor Signaling Promotes the Autophagic Degradation of β-Amyloid Peptide inC. elegans

Florez-McClure¹,

Hohsfield²,

Fonte³

et al. 2007

Autophagy

123

104

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Autophagy is a conserved membrane trafficking pathway that mediates the delivery of cytoplasmic substrates to the lysosome for degradation. Impaired autophagic function is implicated in the pathology of various neurodegenerative diseases. We have generated transgenic C. elegans that express human β-amyloid peptide (Aβ) in order to examine the mechanism(s) of Aβ-toxicity. In this model, Aβ expression causes autophagosome accumulation, thereby mimicking a pathology found in brains of Alzheimer's disease patients. Furthermore, we demonstrate that decreased insulin-receptor signaling [using the daf-2(e1370) mutation] suppresses Aβ-induced paralysis by a mechanism that requires autophagy. Surprisingly, the daf-2 mutation also decreases Aβ-induced autophagosome accumulation. These observations can be explained by a model in which decreased insulin-receptor signaling promotes the maturation of autophagosomes into degradative autolysosomes, whereas Aβ impairs this process. Consistent with this model, we find that RNAi-mediated knock-down of lysosomal components results in enhanced Aβ-toxicity and autophagosome accumulation. Also, Aβ; daf-2(e1370) nematodes contain more lysosomes than either Aβ or control strains. Finally, we demonstrate that decreased insulin-receptor signaling promotes the autophagic degradation of Aβ.

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Section: Do Not Distributementioning

confidence: 78%

Decreased Insulin-Receptor Signaling Promotes the Autophagic Degradation of β-Amyloid Peptide inC. elegans

Florez-McClure¹,

Hohsfield²,

Fonte³

et al. 2007

Autophagy

123

104

View full text Add to dashboard Cite

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“…Assuming similar proportions in C. elegans, we postulated that the DR worms exhibited less muscle mass than the AL-fed worms. Accordingly, previous studies have shown that starvation activates the proteolytic system and leads to the degradation of body wall muscles in C. elegans (Zdinak et al, 1997;Szewczyk et al, 2000;Szewczyk et al, 2002). The observed reduction of the protein content combined with higher locomotory activity is reminiscent of a phenomenon described in penguins and rats.…”

Section: Research Articlementioning

confidence: 82%

Gait-specific adaptation of locomotor activity in response to dietary restriction inCaenorhabditis elegans

Lüersen

Faust

Gottschling

et al. 2014

Journal of Experimental Biology

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Locomotion is crucial for the survival of living organisms, as it allows foraging, flight and mating behaviour. In response to environmental cues, many organisms switch between alternative forms of locomotion, referred to as gaits. The nematode Caenorhabditis elegans exhibits two gaits: swimming in liquids and crawling on dense gels. The kinematics and patterns of muscle activity differ between the two gaits, with swimming being less efficient than crawling. We found that C. elegans when grown on dietary restriction (DR) plates and then tested immediately for swimming activity exhibit an accelerated frequency of body-bending swimming compared with ad libitum-fed worms, resulting in an increased swimming speed. This response is independent of the presence or absence of food bacteria in the assay liquid. In contrast, the crawling speed of DR worms on assay agar plates is decreased and influenced by food availability. Because DR also attenuates the disturbed swimming activity of worms that are deficient in the presynaptic dopamine transporter DAT-1, our data link DR-induced alterations of the swimming gait to synaptic processes. This strongly suggests a biochemical rather than a biomechanical response to DR provoked by changes in the worm's body structure. We conclude that the increase in locomotor activity in response to DR is specific to the swimming gait and might represent a survival strategy, allowing food-deprived nematodes to exit unfavourable environments.

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“…All six transgenic lines made for each promoter plasmid showed the same GFP and LacZ expression patterns. For b-Gal staining, worms in M9 buffer were dried on slides for 10 min, fixed, and permeablized with acetone for 30 min and then incubated overnight with X-Gal (Zdinak et al 1997).…”

Section: Methodsmentioning

confidence: 99%

TheCaenorhabditis elegans ing-3Gene Regulates Ionizing Radiation-Induced Germ-Cell Apoptosis in a p53-Associated Pathway

Luo¹,

Shah²,

Riabowol³

et al. 2009

Genetics

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The inhibitor of growth (ING) family of type II tumor suppressors are encoded by five genes in mammals and by three genes in Caenorhabditis elegans. All ING proteins contain a highly conserved plant homeodomain (PHD) zinc finger. ING proteins are activated by stresses, including ionizing radiation, leading to the activation of p53. ING proteins in mammals and yeast have recently been shown to read the histone code in a methylation-sensitive manner to regulate gene expression. Here we identify and characterize ing-3, the C. elegans gene with the highest sequence identity to the human ING3 gene. ING-3 colocalizes with chromatin in embryos, the germline, and somatic cells. The ing-3 gene is part of an operon but is also transcribed from its own promoter. Both ing-3(RNAi) and ing-3 mutant strains demonstrate that the gene likely functions in concert with the C. elegans p53 homolog, cep-1, to induce germ-cell apoptosis in response to ionizing radiation. Somatically, the ing-3 mutant has a weak kinker uncoordinated (kinker Unc) phenotype, indicating a possible neuronal function.

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Transgene‐coded chimeric proteins as reporters of intracellular proteolysis: Starvation‐induced catabolism of a lacZ fusion protein in muscle cells of Caenorhabditis elegans

Cited by 14 publications

References 31 publications

Decreased Insulin-Receptor Signaling Promotes the Autophagic Degradation of β-Amyloid Peptide inC. elegans

Decreased Insulin-Receptor Signaling Promotes the Autophagic Degradation of β-Amyloid Peptide inC. elegans

Gait-specific adaptation of locomotor activity in response to dietary restriction inCaenorhabditis elegans

TheCaenorhabditis elegans ing-3Gene Regulates Ionizing Radiation-Induced Germ-Cell Apoptosis in a p53-Associated Pathway

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