Chamberlin HM (2000) Curr Biol "Nematode development: An evolutionary fugue."

Chamberlin HM

[Curr Biol, 2000]

Recent studies of vulva development in the nematode Pristionchus pacificus have identified cell interactions that do not appear to occur in Caenorhabditis elegans, The new results underscore the diversity of patterning mechanisms that can produce structures with similar cellular morphology.

Hahn BS et al. (2001) Curr Biol "Tissue integrity: Hemidesmosomes and resistance to stress."

Hahn BS, Labouesse M

[Curr Biol, 2001]

How do animal tissues resist the shearing forces to which they are exposed during locomotion or harsh encounters with the environment? Genetic analysis in Caenorhabditis elegans is furthering our understanding of the nature and function of the attachments that preserve tissue integrity.

Richie CT et al. (2005) Curr Biol "Chromosome segregation: Aurora B gets Tousled."

Golden A, Richie CT

[Curr Biol, 2005]

Aurora B kinases play important roles during mitosis in eukaryotic cells; new work in Caenorhabditis elegans has identified the Tousled kinase TLK-1 as a substrate activator of the model nematode''''s Aurora B kinase AIR-2 which acts to ensure proper chromosome segregation during

Johnson AW et al. (2002) Trends Biochem Sci "Nuclear export of ribosomal subunits."

Johnson AW, Dahlberg J, Lund E

[Trends Biochem Sci, 2002]

The partitioning of cells by a nuclear envelope ensures that precursors of ribosomes do not interact prematurely with other components of the translation machinery. Ribosomal subunits are assembled in nucleoli and exported to the cytoplasm in a CRM1/Ran-GTP-dependent fashion. Export of the large (60S) subunit requires a shuttling adaptor protein, NMD3, which binds to mature, correctly folded subunits. Immature or defective particles do not bind NMD3 and thus are excluded from the export pathway. This structural proofreading is extended into the cytoplasm, where it is believed that several energy-requiring steps release shuttling factors from the subunit, allowing it to function in translation.

Bundy JG et al. (2014) Metallomics "Metabolites and metals in Metazoa--what role do phytochelatins play in animals?"

Bundy JG, Kille P

[Metallomics, 2014]

Phytochelatins are sulfur-rich metal-binding peptides, and phytochelatin synthesis is one of the key mechanisms by which plants protect themselves against toxic soft metal ions such as cadmium. It has been known for a while now that some invertebrates also possess functional phytochelatin synthase (PCS) enzymes, and that at least one species, the nematode Caenorhabditis elegans, produces phytochelatins to help detoxify cadmium, and probably also other metal and metalloid ions including arsenic, zinc, selenium, silver, and copper. Here, we review recent studies on the occurrence, utilization, and regulation of phytochelatin synthesis in invertebrates. The phytochelatin synthase gene has a wide phylogenetic distribution, and can be found in species that cover almost all of the animal tree of life. The evidence to date, though, suggests that the occurrence is patchy, and even though some members of particular taxonomic groups may contain PCS genes, there are also many species without these genes. For animal species that do possess PCS genes, some of them (e.g. earthworms) do synthesize phytochelatins in response to potentially toxic elements, whereas others (e.g. Schistosoma mansoni, a parasitic helminth) do not appear to do so. Just how (and if) phytochelatins in invertebrates complement the function of metallothioneins remains to be elucidated, and the temporal, spatial, and metal specificity of the two systems is still unknown.

Sesti F et al. (2010) Trends Cell Biol "Oxidation of potassium channels by ROS: a general mechanism of aging and neurodegeneration?"

Cai SQ, Liu S, Sesti F

[Trends Cell Biol, 2010]

A wealth of evidence underscores the tight link between oxidative stress, neurodegeneration and aging. When the level of excess reactive oxygen species (ROS) increases in the cell, a phenomenon characteristic of aging, DNA is damaged, proteins are oxidized, lipids are degraded and more ROS are produced, all culminating in significant cell injury. Recently we showed that in the nematode, Caenorhabditis elegans, oxidation of K(+) channels by ROS is a major mechanism underlying the loss of neuronal function. The C. elegans results support an argument that K(+) channels controlling neuronal excitability and survival might provide a common, functionally important substrate for ROS in aging mammals. Here we discuss the implications that oxidation of K(+) channels by ROS might have for the mammalian brain during normal aging, as well as in neurodegenerative diseases such as Alzheimer's and Parkinson's. We argue that oxidation of K(+) channels by ROS is a common theme in the aging brain and suggest directions for future experimentation.

Krupinski T et al. (2009) Physiology (Bethesda) "Unexpected roles of the Na-K-ATPase and other ion transporters in cell junctions and tubulogenesis."

Beitel GJ, Krupinski T

[Physiology (Bethesda), 2009]

Recent work shows that transport-independent as well as transport-dependent functions of ion transporters, and in particular the Na-K-ATPase, are required for formation and maintenance of several intercellular junctions. Furthermore, these junctional and other nonjunctional functions of ion transporters contribute to development of epithelial tubes. Here, we consider what has been learned about the roles of ion pumps in formation of junctions and epithelial tubes in mammals, zebrafish, Drosophila, and C. elegans. We propose that asymmetric association of the Na-K-ATPase with cell junctions early in metazoan evolution enabled vectorial transcellular ion transport and control of intraorganismal environment. Ion transport-independent functions of the Na-K-ATPase arose as junctional complexes evolved.

Blaxter ML et al. (1996) Int J Parasitol "Nematode spliced leaders--ubiquity, evolution and utility."

Blaxter ML, Liu LX

[Int J Parasitol, 1996]

Most nematode messenger RNAs (mRNAs) have at their 5' end a common 22 nucleotide leader sequence, the trans-spliced leader or SL1. The presence of this leader on some but not all mRNAs raises several questions: What is the role of the spliced leader in mRNA maturation, stability and translation? Why do some genes have a spliced leader and others not? What is the evolutionary origin of this trans-splicing mechanism? Recently, additional trans-spliced leaders (SL2, 3, 4, 5) have been described. What role do these variants play in nematode gene expression? While definitive answers to these questions remain elusive, it is clear that the spliced leader will significantly facilitate the cloning and sequence analysis of most nematode mRNAs.

Buckingham, SD et al. (2005) Trends in Pharmacological Sciences "Structure and function of two-pore-domain K+ channels: contributions from genetic model organisms."

Franks, CJ, Buckingham, SD, Law, RJ, Sattelle, DB, Kidd, JF

[Trends in Pharmacological Sciences, 2005]

K+ channels that possess two pore domains in each channel subunit are common in many animal tissues. Such channels are generated from large families of subunits and are implicated in several functions, including temperature sensation, responses to ischaemia, K+ homeostasis and setting the resting potential of the cell. Their activity can be modulated by polyunsaturated fatty acids, pH and oxygen, and some are candidate targets of volatile anaesthetics. However, despite their potential as targets for novel drugs for human health, comparatively little is known about the molecular basis of their diverse physiological and pharmacological properties. Genetic model organisms have considerable potential for improving our understanding of these channels. In this article, we review the contributions of some of these genetic model organisms to recent advances in our knowledge of two-pore-domain K+

Robertson M (1988) Nature "Homoeo boxes, POU proteins and the limits to promiscuity."

Robertson M

[Nature, 1988]

The recent characterization of four proteins, three of them known mammalian transcriptional activators, may do much to diminish the lingering mystique of the homoeo domain and at the same time to focus attention on the role of protein-protein interactions in differential gene expression. The four protein are Oct-2, which is produced in B lymphocytes where it binds to a conserved octamer sequence and activates immunoglobulin genes; Pit-1, which is synthesized in pituitary cells and implicated in the activation of growth-hormone and prolactin genes; unc-86, which has a genetically defined role in the differentiation of specific nematode neural cells; and Oct-1, a ubiquitous mammalian transcriptional activator of small nuclear RNA and histone H2B genes that also acts through a conserved octamer motif.