Picture from Zhang SO et al. (2010) BMC Cell Biol "Lipid droplets as ubiquitous fat storage organelles in C. elegans."

Figure 6. A model of BODIPY and Nile Red trafficking in live wild-type animals and peroxisomal b-oxidation mutants. (A) A schematic diagram of possible BODIPY (green) and Nile Red (red) trafficking in gut epithelial cells in wild-type animals. A single gut epithelial cell is diagrammed as a rectangular box with microvilli (triangles) pointing to the gut lumen. Gut epithelial cells are rich in vesicular structures, which include LROs (orange vesicles), lipid droplets (green vesicles labelled as LD), and other vesiclular organelles (white). Both BODIPY and Nile Red are endocytosed into the gut epithelial cell and trafficked through endolysosomal pathways to LROs (orange arrow and orange vesicles). Hypothetically, BODIPY can be targeted to lipid droplets from LROs and or from endosomes (green arrows question marked). (B) In peroxisomal b-oxidation mutants, lipid droplet size increases (large orange vesicles). Nile Red as well as BODIPY can be targeted to lipid droplets (orange arrows question marked).

Picture from Burmeister C et al. (2008) FASEB J "Oxidative stress in Caenorhabditis elegans: protective effects of the Omega ...."

Figure 4. Analysis of the expression pattern of GSTO-1 in C. elegans. A) Typical expression of GSTO-1::GFP reporter constructs. Weak GFP signals were detected exclusively in the intestinal cells of L1-L4 and adult hermaphrodites. B) Effect of deletion constructs and mutations on GFP expression in gut cells. Worms were microinjected with the constructs GFP-1321, GFP-397, GFP-325, GFP-254, and GFP-178. Fluorescence was observed in transgenic worms expressing the constructs GFP-397 and GFP-325 (as indicated in green). No signal was obtained for the shorter constructs GFP-254 and GFP-178. To investigate the involvement of the GATA element 259-265 bp upstream of the initiation codon (as indicated in red) in regulating transcription, site-directed mutagenesis was used. Mutation resulted in complete loss of GFP expression. C) Immunogold electron microscopy. Part of a cross section of wild-type worms using preimmune (A) and anti-GSTO-1 antibody (B). LD = lipid droplet; MT = mitochondria; IL = inner lumen of intestine; GP = gold particle. Electron micrographs were taken on a Phillips CM-10 transmission electron microscope.

Picture from Warner A et al. (2011) Mol Biol Cell "The Caenorhabditis elegans paxillin orthologue, PXL-1, is required for ...."

Figure 4: Confirmation of protein interactions and immunostaining with a PXL-1 antibody (A). Screening by the yeast two-hybrid method of a collection of 30 known components of dense bodies and M-lines revealed that the six indicated proteins interact with PXL-1. By domain mapping, the LD motif region is sufficient for interaction with DEB-1 (vinculin) and LIM-8, and the LIM domain region is sufficient for interaction with UNC-95 and UIG-1 (a Cdc42 GEF). UNC-96 and HUM-6 are also able to bind to PXL-1. (B) These interactions, except that with HUM-6, were verified using purified proteins. Yeast-expressed HA-tagged PXL-1 was precipitated with anti-HA beads, washed, incubated with bacterially expressed MBP of the indicated MBP fusion proteins, and washed, and the eluted proteins were separated on a gel, blotted, and reacted with either anti-MBP or anti-HA. All tested proteins except UNC-96 showed conclusive results, with a faint band observed in 5B when reacted with anti-MBP. A paxillin (PXL-1) polyclonal rabbit antibody was produced to detect PXL-1 in C. elegans as well as in yeast expressing HA-PXL-1. PAT-3/β-integrin (GFP; Ci) is a major component of dense bodies, M-lines, and attachment plaques, and the PXL-1 antibody (Cii) clearly colocalizes with PAT-3/²-integrin in dense bodies and adhesion plaques (Ciii). The PXL-1 antibody also stains M-lines, but very weakly (not shown). Paxillin from the nematode lysate displays a slower mobility than that of nematode paxillin expressed in yeast (see Discussion) (D). Bar, 2 μm.