Pruyne, David et al. (2015) International Worm Meeting "Roles for formins in the development and function of muscle and myoepithelial cell types."

Hegsted, Anna, Mi-Mi, Lei, Votra, SarahBeth, Pruyne, David, Wright, Forrest

[International Worm Meeting, 2015]

Formins are highly conserved regulators of actin filament dynamics. In vitro, formins stimulate the nucleation of actin filaments from monomers, and frequently enhance the rate of filament elongation, resulting in the formation of long, unbranched actin filaments. Using C. elegans as a model to identify in vivo functions of formin homologs, we have discovered that these proteins contribute to the function of several distinct cell types with contractile activity. The formins encoded by cyk-1 and fhod-1 contribute to the growth of striated body-wall muscle, while the formin encoded by exc-6 is required for the proper behavior of myoepithelial cells of the spermatheca during ovulation. In each of these cases, the formin proteins are physically associated with actin filament-rich contractile structures, but these actin-containing structures are not lost in mutants for these formin genes, suggesting these formins might not simply direct the assembly of contractile structures. Rather, microscopic and biochemical analysis of these mutants suggest some of these formins may play more subtle roles in modulating actin filament dynamics, or possibly even affect the expression of other contraction-related genes.

Pruyne, David et al. (2010) C. elegans: Development and Gene Expression, EMBL, Heidelberg, Germany "Exploring Formin Functions in Worm Muscles."

Bretscher, Anthony, Kemphues, Kenneth, Mi-Mi, Lei, Pruyne, David

[C. elegans: Development and Gene Expression, EMBL, Heidelberg, Germany, 2010]

By far, the largest population of actin filaments in most multicellular animals is those that constitute the contractile apparatus of muscle cells, yet little is known of how these filaments are assembled in vivo . Studies of vertebrate cultured muscle cells have implicated a conserved family of cytoskeletal regulatory proteins called Formins as putative muscle actin assembly factors, specifically identifying Formins of the Formin HOmology Domain (FHOD) subfamily as important to this. C. elegans encodes a single FHOD homolog, FHOD-1. We find that this well-conserved FHOD homolog is a muscle-specific Formin, but in surprising contrast to what has been described for cultured cells, loss of FHOD-1 in intact animals results in only modest defects in muscle actin organization in a subset of muscle cells. Despite this mild phenotype, the subcellular distribution of FHOD-1 is consistent with a role for this Formin in helping direct the assembly and organization of contractile actin filaments in worm muscle cells. As one ongoing approach, we are searching for factors that might function redundantly with FHOD-1 in assembly of this large pool of actin filaments.

Zarkower D et al. (1994) Worm Breeder's Gazette "mab-3 YAC Rescue"

De Bono M, Hodgkin JA, Zarkower D

[Worm Breeder's Gazette, 1994]

mab-3 YAC rescue David Zarkower, Mario de Bono, and Jonathan Hodgkin MRC Laboratory of Molecular Biology, Cambridge, England

Mi-Mi, Lei et al. (2013) International Worm Meeting ""Ultrastructure analysis of the sarcomeres in worms that lack Z-line formins"."

Pruyne, David, Mi-Mi, Lei

[International Worm Meeting, 2013]

Even with extensive studies that revolve around actin cytoskeleton, the detailed mechanism as to how actin filaments are recruited into sarcomeres, the smallest units of striated muscle contractile lattice, is yet to be elucidated. The barbed ends of actin filaments anchor at the Z-line structures (dense bodies in C. elegans) that define the sarcomere ends. Net actin polymerization favorably occurs at the barbed end that is known to have unique association with formins, one of the highly conserved and most widespread families of actin nucleating factors. We have shown in our previous study that two nematode formins, CYK-1 and FHOD-1 are Z-line-associated proteins that work together to organize and maintain sarcomeric organization in C. elegans striated muscle - the first evidence in an intact organism. In this study, we have carried out the ultrastructure analysis on sarcomeric structures of worms lacking CYK-1 and/or FHOD-1. Not only do the current electron microscopy results complement our previous conclusions, they also suggest that CYK-1 and/or FHOD-1 may contribute in achieving normal Z-line structures in C. elegans sarcomeric organization.

Weinkove D (2018) BMC Biol "On microbes, aging and the worm: an interview with David Weinkove."

Weinkove D

[BMC Biol, 2018]

David Weinkove is an associate professor at Durham University, UK, studying host-microbe interactions in the model organism Caenorhabditis elegans. David has been focusing on the way microbes affect the physiology of their hosts, including the process of aging. In this interview, he discusses the questions shaping his research, how they evolved over the years, and his guiding principles for leading a lab.

Miller DM et al. (1992) Worm Breeder's Gazette "unc-4 LacZ Expression in A-Type Motor Neurons"

Miller DM, Niemeyer CJ

[Worm Breeder's Gazette, 1992]

unc-4 LacZ expression in A-type motor neurons David M. Miller and Charles J. Niemeyer, Dept. of Cell Biology, Duke Univ. Medical Ctr, Durham, NC 27710

Hegsted, Anna et al. (2015) International Worm Meeting "The formin EXC-6/INFT-1 is required for normal ovulation."

Pruyne, David, Hegsted, Anna, Wright, Forrest

[International Worm Meeting, 2015]

Actin cytoskeleton organization is important for proper function of the Caenorhabditis elegans gonad, especially contractility of the spermatheca. Aberrant actin organization in the spermatheca has been linked to contractility deficiencies and calcium signaling defects leading to improper ovulation. Formins are actin nucleation factors, and many promote the elongation of unbranched actin filaments. In the absence of the formin EXC-6/INFT-1, worms lay fewer eggs than wild type. These worms also exhibit aberrant ovulation. Further investigation shows that INFT-1 is expressed in the spermatheca and partially colocalizes with actin filament bundles. Due to the role of INFT-1 in proper ovulation and its localization, we hypothesize that INFT-1 is important for spermatheca actin organization and/or spermatheca calcium signaling. .

Grenache DG et al. (1993) Worm Breeder's Gazette "Differential Effects of Dauer-Defective Mutations in L1-Specific Surface Antigen Switching"

Politz SM, Grenache DG

[Worm Breeder's Gazette, 1993]

DIFFERENTIAL EFFECTS OF DAUER-DEFECTIVE MUTATIONS ON L1- SPECIFIC SURFACE ANTIGEN SWITCHING. David G. Grenache and Samuel M. Politz, Department of Biology and Biotechnology, Worcester Polytechnic Institute, Worcester, MA.

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

Emmons SW, Fitch DHA, Leroi AM

[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

Hall DH et al. (1994) Worm Breeder's Gazette "Cytology of Degenerin-Induced Cell Death in the PVM Neuron"

Driscoll MA, Chalfie M, Gu GQ, Hall DH, Gong L

[Worm Breeder's Gazette, 1994]

Cytology of degenerin-induced cell death in the PVM neuron David H. Hall, Guoqiang Gu+, Lei Gong#, Monica Driscoll#, and Martin Chalfie+, * Dept. Neuroscience, Albert Einstein College of Medicine, Bronx, N.Y. 10461 + Dept. Biological Sciences, Columbia University, New York, N.Y. 10027 # Dept. Molecular Biology and Biochemistry, Rutgers University, Piscataway, N.J. 08855