Nathan, Sara et al. (2015) International Worm Meeting "Identifying and characterizing odor receptors in C. elegans."

Cox-Harris, Alesha, Brueggemann, Chantal, Mosqueda, Berenice, Young, Jared, Newman, Elizabeth, Nathan, Sara, Morton, Riva, Dalton, Cassidy, L'Etoile, Noelle, Apostol, Sherrlyne

[International Worm Meeting, 2015]

Although scientists have been studying olfaction in C. elegans for decades, olfactory receptor proteins remain largely uncharacterized. To address this knowledge gap, we are pursuing localization of candidate odor receptor proteins, and studying odor responses in genetically altered worms. We are producing lines with GFP-tagged putative odor receptors using constructs obtain from the Transgeneome project, and looking for proteins that localize to sensory cilia. We are testing chemotaxis to a variety of odors of worms in which expression of putative odor receptors have been reduced using RNA interference. We are also generating knockout worms for putative odor receptors using the CRISPR technique, to be tested in chemotaxis assays. .

Warnhoff, Kurt et al. (2021) International Worm Meeting "Interkingdom transfer of molybdenum cofactor from bacteria to C. elegans"

Hercher, Thomas, Warnhoff, Kurt, Ruvkun, Gary, Mendel, Ralf

[International Worm Meeting, 2021]

The molybdenum cofactor (Moco) is a 520 dalton prosthetic group that is synthesized in a multi-step enzymatic pathway present in Archaea, Bacteria, and Eukarya. In animals, four oxidases (among them sulfite oxidase) use Moco as a prosthetic group. Moco is essential in animals; humans with mutations in genes that encode Moco-biosynthetic enzymes display lethal neurological and developmental defects. Moco supplementation seems a logical therapy, however free Moco is too fragile to be purified and administered therapeutically. Surprisingly, Moco biosynthesis is not essential in the nematode Caenorhabditis elegans if they are fed bacteria that synthesize Moco. Our genetic and biochemical studies demonstrate that protein-bound Moco is the stable, bioavailable species of Moco taken up by C. elegans from bacteria and is an effective dietary supplement in a C. elegans model of Moco deficiency. These findings establish an animal pathway for Moco transport and suggest a novel therapeutic strategy for Moco deficiency.

Aamodt SJ et al. (1995) International C. elegans Meeting "TAU-1, A MICROTUBULE-ASSOCIATED PROTEIN THAT MAY CONNECT MICROTUBULES TO MEMBRANES"

McDermott JB, Aamodt EJ, Aamodt SJ

[International C. elegans Meeting, 1995]

The tau microtubule-associated proteins (MAPs) are an extensively studied class of microtubule-binding proteins that are located in axons. Microtubules isolated from C. elegans contain several proteins that are similar to vertebrate taus in size and antigenicity. The genome sequence revealed a predicted gene, tau-1, that has homology to mammalian tau. tau-1 may encode a 57,000 Dalton protein with four domains: a transmembrane domain encoded by exon 1; an acidic, proline-rich domain encoded by exon 2; an extended arm-like domain encoded by exons 3 and 4; and a tau-like microtubule binding domain encoded by exons 5, 6 and 7. The properties of mammalian tau appear to be regulated by phosphorylation. TAU-1 has 15 predicted phosphorylation sites and 4 potential glycosylation sites. Southern blots indicate that there is only one sequence in the C. elegans genome closely homologous to the first exon of tau-1. Computer analysis suggests that tau-1 encodes a class IIIa transmembrane protein and tau-1 may represent a new class of microtubule binding proteins that link microtubules to membranes. This class of microtubule-associated proteins would not be isolated in standard MAP preparations. We are making fusion genes and antibodies to determine where tau-1 is expressed and its intracellular location.

Bergstrom AR et al. (1991) International C. elegans Meeting "IDENTIFICATION OF A Gj-LlKE PROTEIN IN C. ELEGANS MEMBRANES: POSSIBLE ROLE IN POLYAMINE METABOLISM."

Schaeffer JM, Bergstrom AR

[International C. elegans Meeting, 1991]

Guanine nucleotide-binding regulatory proteins (G-proteins) represent a family of trimeric proteins which mediate communication between a variety of cell surface receptors and effector molecules such as adenylate cyclase, phosphoinositol-specific phospholipase C and ion channels. When an appropriate agonist binds to a G protein- linked receptor, the alpha subunit of the G protein is activated and binds GTP resulting in a dissociation of the three G protein subunits. The intrinsic GTPase activity of the alpha subunit hydrolyzes GTP to GDP and the subsequent GDP-alpha subunit recombines with the other two G protein subunits ending the activation cycle. There are both stimulatory- and inhibitory-G proteins which are specifically ribosylated by bacterial toxins. We have identified and characterized a 41,000 dalton protein from C. elegans membranes with properties similar to previously described Gj-like proteins. Our laboratory previously presented evidence that specific dibenzoguanidines (and structural analogs including robenidine) are potent inhibitors of C. elegans ornithine decarboxylase, possibly acting via a G-protein. Consequently, the effect of robenidine on pertussis toxin stimulated ADP-ribosylation and GTPase activity in C. elegans has been evaluated. As shown in this poster, robenidine is a potent inhibitor of pertussis toxin-mediated ADP-ribosylation and stimulator of GTPase activity. Further work is required to determine whether there is a direct link between this Gj-like protein and ODC activity.