Zhao C et al. (1993) Worm Breeder's Gazette "Cloning of the lin-32 Gene"

Emmons SW, Zhao C

[Worm Breeder's Gazette, 1993]

Cloning of the lin-32 gene Connie Zhao and Scott W. Emmons, Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461

Townsend SR et al. (1994) Worm Breeder's Gazette "C. elegans Molecular Genetics and Long PCR."

Savage C, Padgett RW, Finelli AL, Xie T, Townsend SR

[Worm Breeder's Gazette, 1994]

C. elegans Molecular Genetics and Long PCR Scott R. Townsend, Cathy Savage, Alyce L. Finelli, Ting Xie, and Richard W. Padgett, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855

Eve A (2021) Development "An interview with Swathi Arur."

Eve A

[Development, 2021]

Swathi Arur is an Associate Professor for the Department of Genetics at the MD Anderson Cancer Center, USA, where she uses multidisciplinary approaches to understand female germline development and fertility. She has received numerous accolades, including the MD Anderson Distinguished Research Faculty Mentor Award in 2017. In 2020, she was elected to the American Association for the Advancement of Science (AAAS). Swathi joined the team at Development as an Academic Editor in 2020, and we met with her over Zoom to hear more about her life, her career and her love for <i>C. elegans</i>.

Emmons SW et al. (1994) Worm Breeder's Gazette "Strain Names for non-C. elegans Species."

Emmons SW, Leroi AM, Fitch DHA

[Worm Breeder's Gazette, 1994]

Strain names for non-C. elegans species Scott W. Emmonst, Armand Leroit, and David Fitch, Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461, Department of Biology, New York University, RmlOO9 Main Bldg., Washington Square, New York, NY 10003

Dixon JR (2019) Dev Cell "TADs for Life: Chromatin Domain Organization Regulates Lifespan in C.elegans."

Dixon JR

[Dev Cell, 2019]

In this issue of Developmental Cell, Anderson etal. (2019) show that chromatin domain structure on the X chromosome in C.elegans is dispensable for dosage compensation but regulates longevity and thermotolerance. This study sheds light on the mechanisms of domain formation in C.elegans and how these features affect physiology.

Vrbanac A et al. (2017) Cell Host Microbe "An Elegan(t) Screen for Drug-Microbe Interactions."

Dorrestein P, Morton JT, Debelius JW, Knight R, Jiang L, Vrbanac A

[Cell Host Microbe, 2017]

Microbes affect drug responses, but mechanisms remain elusive. Two papers in Cell exploit C.elegans to infer anticancer drug mechanisms. Through high-throughput screens of drug-microbe-host interactions, Garcia-Gonzalez etal. (2017) and Scott etal. (2017) determine that bacterial metabolism underpins fluoropyrimidine cytotoxicity, providing a paradigm for unraveling bacterial mechanisms in drug metabolism.

Alexander Gottschalk et al. (2003) International Worm Meeting "Tandem affinity purification of the levamisole receptor, mass spectrometric identification and functional characterization of associated proteins"

William Schafer, Scott Anderson, Alexander Gottschalk, John Yates

[International Worm Meeting, 2003]

Nicotinic acetylcholine receptors (nAChRs) mediate excitatory neurotransmission at neuron/neuron and neuron/muscle synapses. Little is known about proteins accessory to nAChRs, which may control their functional properties and thus play a role in nicotine addiction. To identify such proteins, we performed tandem affinity purification (TAP) of the levamisole receptor, a nAChR expressed in muscles and neurons. Proteins in the unseparated eluate were analyzed after tryptic digest by liquid chromatography / electrospray tandem mass spectrometry. Among the abundant proteins present were the nAChR subunits UNC-29, LEV-1, UNC-38 and UNC-63, previously implicated in formation of the levamisole receptor by genetics and electrophysiology. In addition, we found the -type nAChR subunits ACR-8, ACR-12 and ACR-13. A Tc1-insertion in acr-8 confers nicotine resistance, just like mutations in the previously known levamisole receptor genes, while a deletion in acr-12 does not. GFP-fusions of ACR-8 and ACR-13 are expressed in muscles and neurons, whereas ACR-12 is exclusively neuronal. The novel subunits may thus be components of distinct sub-populations of the levamisole receptor, possibly replacing the -subunits UNC-38 and/or UNC-63. Consistently, ACR-8 and ACR-12 co-localize in post-synaptic receptor clusters with UNC-38, while UNC-38 is also present in clusters not containing ACR-8 or ACR-12. Many other proteins were co-purified with the levamisole receptor, among them the calcineurin A subunit TAX-6 and calmodulin (CMD-1). Calcineurin is a Ca2+-activated phosphatase comprising catalytic A and regulatory B subunits, as well as calmodulin. Vertebrate calcineurin was found to reduce the rate by which nAChRs recover from agonist-induced desensitization. Consistently, tax-6(p675) and cnb-1(jh103) mutants (calcineurin B subunit), or animals in which calmodulin was knocked down by RNAi, are hypersensitive to nicotine. TAX-6::GFP and antibody-labeled UNC-38 are found in the same nervecord processes, in agreement with a direct interaction. To address possible functions in cholinergic neurotransmission of other proteins co-purified with the levamisole receptor, we are using RNAi. So far, of 12 candidates that we knocked down by RNAi, 5 exhibit increased sensitivity to nicotine. We are further assessing possible changes of levamisole receptor abundance and localization in these knock-down animals.

Greenwald IS et al. (1983) Worm Breeder's Gazette "Tc1 polymorphisms on the right arm of LGIII."

Hodgkin JA, Greenwald IS

[Worm Breeder's Gazette, 1983]

As starting points for the molecular cloning of lin-12 III and tra-1 III, we have identified several Tc1 polymorphisms linked to these genes. Genomic DNA was prepared from appropriate Bristol/Bergerac hybrid strains, cut with EcoRI, and probed with Tc1 (kindly provided by Scott Emmons). Our data are summarized in the maps below, which give the approximate map locations and EcoRI fragment sizes of the Bergerac-specific Tc1's. [See Figure 1]

Sood P et al. (2017) Traffic "Cargo crowding at actin-rich regions along axons causes local traffic jams."

Kumar TV, Koushika SP, Murthy K, Sood P, Menon GI, Nonet ML

[Traffic, 2017]

Steady axonal cargo flow is central to the functioning of healthy neurons. However, a substantial fraction of cargo in axons remains stationary up to several minutes (Kang, Tian et al. 2008, Tang, Scott et al. 2012, Tang, Scott et al. 2013, Iacobucci, Rahman et al. 2014). We examine the transport of precursors of synaptic vesicles (pre-SVs), endosomes and mitochondria in C. elegans touch receptor neurons (TRNs), showing that stationary cargo are predominantly present at actin-rich regions along the neuronal process. Stationary vesicles at actin-rich regions increase the propensity of moving vesicles to stall at the same location, resulting in traffic jams arising from physical crowding. Such local traffic jams at actin-rich regions are likely to be a general feature of axonal transport since they also occur in Drosophila neurons. Repeated touch stimulation of C. elegans reduces the density of stationary pre-SVs, indicating that these traffic jams can act as both sources and sinks of vesicles. This suggests that vesicles trapped in actin-rich regions are functional reservoirs that may contribute to maintaining robust cargo flow in the neuron.

Yung S Lie et al. (2002) West Coast Worm Meeting "Identification of proteins interacting with MIG-13 in Q cell migration"

Scott Anderson, Yung S Lie, Cynthia Kenyon, John R Yates

[West Coast Worm Meeting, 2002]

We are studying cell migration in the context of anteroposterior migrations of the Q neuroblasts and their descendants. QR and QL are born in right-left symmetrical positions in the animal. QR and its descendants migrate towards the anterior of the body, while QL and its descendants migrate towards the posterior. Proper positioning of QR and its descendants in the anterior requires mig-131 . Interestingly, mig-13 functions non cell-autonomously to specify the stopping point of migrating cells but is not associated with any specific landmark1 . mig-13 encodes a novel transmembrane protein1 . We currently know very little about the mechanism by which MIG-13 functions. In order to learn more about how migrating cells determine a final stopping point, we are performing biochemical experiments to isolate proteins that bind to MIG-13. Immunoprecipitations were performed using extracts from worms expressing a rescuing GFP-MIG-13 fusion, or as a control, from worms expressing GFP alone. A commercial anti-GFP antibody was used to isolate the fusion protein (or GFP alone in the control) and any associated proteins. Immunoprecipitated samples were analyzed by mass spectrometry to identify proteins present in each sample. We will present preliminary data from this mass spectrometry analysis. Identification of proteins interacting with MIG-13 will enable us to perform further biochemical experiments to characterize these interactions; in addition, we will be able to test the functional significance of these protein-protein interactions using RNAi or other genetic approaches.