Bandyopadhyay J et al. (2004) Mol Cells "Regulation of calcineurin, a calcium/calmodulin-dependent protein phosphatase, in C. elegans."

Lee J, Bandyopadhyay J, Bandyopadhyay A

[Mol Cells, 2004]

Calcineurin is a calcium/calmodulin-dependent serine/ threonine protein phosphatase. It is a heterodimeric protein consisting of a catalytic subunit calcineurin A, and a regulatory calcium-binding subunit, calcineurin B. The primary sequence of both subunits and heterodimeric structure is highly conserved from yeast to mammals. Calcineurin has long been implicated in various signaling pathways. Calcineurin genes (cna-1/tax-6 and cnb-1) have been identified in the nematode Caenorhabditis elegans, which share high homology with their Drosophila and mammalian counterparts. C. elegans calcineurin binds calcium and functions as a heterodimeric protein phosphatase establishing its biochemical conservation. Calcineurin expresses in diverse tissues implicating its important role in various physiological processes. This review will focus in brief on the expression pattern and regulation of calcineurin including its effect on growth and development, locomotion, egg-laying, and sensory responses.

Hodgkin JA (1998) International Journal of Developmental Biology "Seven types of pleiotropy."

Hodgkin JA

[International Journal of Developmental Biology, 1998]

Pleiotropy , a situation in which a single gene influences multiple phenotypic tra its, can arise in a variety of ways. This paper discusses possible underlying mechanisms and proposes a classification of the various phenomena involved.

Wong C et al. (2003) Curr Biol "Dispatch. Centrosome biology: a SAS-sy centriole in the cell cycle."

Wong C, Stearns T

[Curr Biol, 2003]

A novel protein in Caenorhabditis elegans, SAS-4, is a component of centrioles and is required for centriole duplication. Depletion of SAS-4 results in stunted centrioles and a smaller centrosome, suggesting a link to organelle size control.

Hall PA et al. (1997) Curr Biol "Tumor suppressors: a developing role for p53?"

Hall PA, Lane DP

[Curr Biol, 1997]

An increasing body of evidence indicates that p53, the product of a tumour suppressor gene, has a role in development - could this developmental role have provided the primary driving force in the evolution of a protein best known as a stress-response integrator?

Smidt MP et al. (2009) Genome Biol "A passport to neurotransmitter identity."

Burbach JP, Smidt MP

[Genome Biol, 2009]

Comparison of a regulatory network that specifies dopaminergic neurons in Caenorhabditis elegans to the development of vertebrate dopamine systems in the mouse reveals a possible partial conservation of such a network.

Bourne HR et al. (1990) Nature "Some signal developments."

Kenyon CJ, Bourne HR, Wrischnik LA

[Nature, 1990]

What molecular signalling machines tell a precursor cell to develop into a specialized structure? In one case, described in three papers, including that by Aroian et al. on page 693 of this issue, these machines turn out to be a receptor tyrosine kinase and a ras protein.

Moss EG (2000) Curr Biol "Non-coding RNAs: Lightning strikes twice."

Moss EG

[Curr Biol, 2000]

A second case has been found of a nematode gene involved in developmental timing that encodes a short, non-coding RNA. Both RNAs are expressed at specific times and appear to repress target genes by interacting with their 3' untranslated regions. A coincidence? Or does this pathway attract small RNA regulators?

Miller DM et al. (1986) "The sup-3 locus is closely linked to a myosin heavy chain gene in C. elegans."

Miller DM, Maruyama IN

[1986]

C. elegans body wall muscle thick filaments are assembled from two different types of myosin heavy chain, MHC A and MHC B. The structural gene for the MHC A protein has been identified from the reaction of bacterial fusion peptides with specific monoclonal antibodies. We have also shown that a mutation in the sup-3 locus that enhances the accumulation of the MHC A protein is closely linked to the MHC A gene. A model of sup-3 action is proposed.

Chamberlain JS et al. (2000) Curr Biol "Muscular dystrophy: the worm turns to genetic disease."

Chamberlain JS, Benian GM

[Curr Biol, 2000]

A new animal model for studying muscular dystrophy, a mutant form of the nematode Caenorhabditis elegans, brings the power of worm genetics to bear on the search for a cure for this disease; work on this worm has already led to the identification of a novel component that can suppress the mutant phenotype.

Severson AF et al. (2002) Dev Cell "Cytokinesis: Closing in on the central spindle."

Severson AF, Bowerman B

[Dev Cell, 2002]

The central spindle is important for the completion of cytokinesis. Genetic and biochemical approaches have identified a tetrameric complex, made up of a mitotic kinesin-like protein and a Rho-GTPase activating protein, that mediates central spindle assembly.