Picture from Ji N et al. (2013) Cell "Feedback control of gene expression variability in the Caenorhabditis elegans ...."

Figure 1. Using Single-Cell Transcript Counting to Study the Control of mab-5 Expression (A) Schematic representation of the activation of MAB-5 expression in QL in response to the posterior- to-anterior gradient of EGL-20/Wnt. (B) Model of Wnt signaling based on published studies. Question marks and gray edges indicate lack of definitive evidence. (C) Final position of QL descendants in wild-type and various Frizzled loss-of-function mutants. Unless otherwise noted, compound mutants carry the same alleles as single mutants. (D) Detection of mab-5 transcripts using smFISH over the course of QL migration. Upper: QL at different stages of its migration. V5 is a stationary cell used as spatial reference. Lower: smFISH staining of mab-5 transcripts in the same cells as shown above. Yellow arrowheads: single mab-5 transcripts; white arrowheads: transcription centers in the nucleus. Scale bar represents 2.5 mm. (E) mab-5 transcription dynamics in single QL neuroblasts in wild-type animals. Upper: normalized total MD for worms collected at different time points after hatching. Black dots mark the mean, and blue bars span 2.5-97.5 percentiles. Lower: number of mab-5 transcripts per cell plotted against MD. The histogram to the right is generated using data points to the left with MD > 8. Black lines are generated by fitting to a sigmoidal function. Red curves are generated by fitting with two Gaussian distributions. (F) mCherry transcription dynamics in the POPTOP strain.

Picture from Yoshina S et al. (2015) PLoS One "Loss of C. elegans GON-1, an ADAMTS9 Homolog, Decreases Secretion Resulting in ...."

Fig 6. Depletion of gon-1 causes DAF-7 secretion defects. (a, b) Fluorescent images of DAF-7::mCherry, and DIC images (inset) in the head neurons of a wild-type animal (a) and a gon-1(tm3146) mutant animal (b) (160 msec. exposure time). The scale bar indicates 10 um. (c) Quantification of the mCherry fluorescence in neurons. The graph represents the combined results of 3 independent experiments (n > 20 neurons per strain). *p < 0.05. Bars represent themean SE. (d, e) Representative fluorescent images of DAF-7::mCherry in the coelomocytes of wild-type (d) and a gon-1(tm3146) mutant (e) animals (100 msec. exposure time). Coelomocytes are outlined with dotted circles in the fluorescent images. Insets show DIC images. The scale bar indicates 10 um. (f) Quantification of the mCherry fluorescence in coelomocytes. The graph represents the combined results of 3 independent experiments (n > 30 coelomocytesper strain). Fluorescence intensity was examined using ImageJ (NIH, Bethesda, MD). *p < 0.05. Bars represent the mean SE.IL is WBbt:0003888" Certain

Picture from Yoshina S et al. (2022) MicroPubl Biol "Integration of multicopy extrachromosomal transgenes into defined loci ...."

Figure 1. Isolation of multicopy integrant strains by the CRISPR/Cas9 system.(A) Procedures for isolation of multicopy integrant strains by the CRISPR/Cas9 system. Fluorescent markers are shown by green (EGFP) and red (DsRed). (B) Relative amounts of the lag-2 promoter and the T07F10.1 gene as determined by quantitative PCR. Primer set 1 is targeted at the lag-2 promoter. Primer set 2 is targeted at the T07F10.1 gene. The data were normalized with the ama-1 gene. The copy numbers are presented as a ratio to the wild-type N2 (n>3). (C) A scatter plot of the copy number of integrated sequences (abscissa) against fluorescence intensity (ordinate) in the Ex5672, and the 14 Is lines. The X axis is shown in log scale. The graph represents the intensity of fluorescence of DTC (y-axis, n > 20 animals per strain). Fluorescence intensity was measured using ImageJ (NIH, Bethesda, MD). (D) Example of GFP protein expressed in DTC. Scale bar = 5.0 μm. (2 sec. exposure time, gain X 4)

Picture from Rolland, Stephane et al. (2022) MicroPubl Biol

Figure 1. Genetic screen identifies additional proteins involved in the maintenance of mitochondrial homeostasis. A. The candidates identified in the screen are listed by functional groups. When available, the name of the human ortholog as stated on Alliancegenome.org is indicated. Protein localization is indicated and is based on experimental evidence in C. elegans or experimental evidence using the human ortholog. In case no experimental evidence was available, the localization was predicted with the PSORT II website (https://psort.hgc.jp/form2.html). Newly identified candidates are indicated in green whereas candidates identified in previous genetic screens are indicated in blue (Runkel et al. 2013, Bennett et al. 2014).Finally, candidates identified in a previous genetic screen for enhancers of fzo-1(tm1133lf)-induced UPRmt are indicated in yellow (Haeussler et al. 2021). B. DIC and fluorescence images of animals carrying the hsp-6p::GFP (zcIs13) reporter and either homozygous for the C25H3.11 loss-of-function allele ok2632 (C25H3.11(ok2632)) or homozygous wildtype for C25H3.11 (mIn1/mIn1). The balancer mIn1 carries the dpy-10(e128) mutation and the pharyngeal myo-2p::GFP transgene, which is visible in the mIn1/mIn1 Dumpy animal (indicated by an arrow in the right panel). Induction of the hsp-6p::GFP reporter is visible in the intestine of C25H3.11(ok2632) homozygous animals (indicated by an arrowhead in the right panel) but not in animals homozygous for the balancer mIn1. C. Wild-type (+/+) and C25H3.11(ok2632) animals were analyzed by Western analysis using anti-tubulin (loading control) and anti-GFP antibodies. D. C25H3.11 VPS13D has been proposed to be a conduit that transfers lipids between ER and mitochondria and between ER and peroxisomes (Guillen-Samander et al. 2021). It localizes to the ER in a VPR-1 VAP-B dependent manner (Guillen-Samander et al. 2021). PRX-3 PEX3 and PRX-12 PEX12 are essential for peroxisome biogenesis and hence peroxisomal beta oxidation (Petriv et al. 2002). Inactivation of any of thesegenes induces the expression of the hsp-6p::GFP reporter and hence triggers UPRmt, indicating that these proteins are required to maintain mitochondrial homeostasis.