Adams JM et al. (2002) Curr Opin Cell Biol "Apoptosomes: engines for caspase activation."

Adams JM, Cory S

[Curr Opin Cell Biol, 2002]

Activation of the caspases that initiate apoptosis typically requires cognate scaffold proteins, including CED-4 in Caenorhabditis elegans, Apaf-1 in mammals and Dark in Drosophila. Each scaffold protein oligomerizes procaspases into a complex called the apoptosome, but the regulation and biological roles of the scaffolds differ. Whereas CED-4 is restrained by the Bcl-2 homologue CED-9, Apaf-1 is inhibited by its WD40 repeat region, until it is activated by cytochrome c, derived from damaged mitochondria. Although Dark also has a WD40 region, its activation does not seem to involve cytochrome c. CED-4 is essential for apoptosis in the worm and Dark for many apoptotic responses in the fly, but the Apaf-1/caspase-9 system probably amplifies rather than initiates the

Adam Antebi (2006) WormBook "Nuclear hormone receptors in C. elegans."

Adam Antebi

[WormBook, 2006]

Nuclear receptors (NRs) are transcription factors typically regulated by lipophilic hormones, which coordinate metazoan metabolism, development and homeostasis. C. elegans has undergone a remarkable expansion of the family, harboring 284 of these receptors in its genome. Approximately 20 of them have been analyzed genetically, most of which correspond to conserved homologs in other metazoans. These NRs variously affect broad life history traits such as sex determination, molting, developmental timing, diapause, and life span. They also impact neural development, axon outgrowth and neuronal identity. Finally, they influence lipid and xenobiotic metabolism. The study of C. elegans NRs holds great promise for dissecting nuclear receptor signaling pathways in vivo in the context of complex endocrine networks.

Adam SA (2009) Semin Cell Dev Biol "The nuclear transport machinery in Caenorhabditis elegans: A central role in morphogenesis."

Adam SA

[Semin Cell Dev Biol, 2009]

Our full understanding of the various roles for the nuclear transport machinery has come from a variety of model organisms including yeast, nematodes, fruit flies and vertebrates. Using the nematode Caenorhabditis elegans, it has been shown that the karyopherin family of nuclear transporters and the components of the Ran cycle have roles not only in nuclear protein transport, but also in mitotic spindle formation and regulation, and in nuclear envelope assembly. These studies have also demonstrated a role for nuclear transport factors in cellular differentiation and development, particularly for the formation of germ cells. This review highlights the small number of studies in C. elegans that have been critical to our understanding of this important cellular process.

Primakoff P et al. (2000) Trends Genet "The ADAM gene family: surface proteins with adhesion and protease activity."

Primakoff P, Myles DG

[Trends Genet, 2000]

An ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain and, therefore, it potentially has both cell adhesion and protease activities. Currently, the ADAM gene family has 29 members, although the function of most ADAM gene products is unknown. We discuss the ADAM gene products with known functions that act in a highly diverse set of biological processes, including fertilization, neurogenesis, myogenesis, embryonic TGF-alpha release and the inflammatory response.

Adam M et al. (2002) M S-Medecine Sciences "Genetic approaches to programmed cell death: achievements and questions."

Golstein P, Adam M, Levraud JP

[M S-Medecine Sciences, 2002]

A useful approach to study molecular mechanisms of cell death is, classically, mutagenesis followed with identification of the altered gene. For caspase-dependent cell death, this has provided spectacular results in the nematode C. elegans more than in other organisms. Often different molecules have been identified as a function of the investigated organism. These differences reflect, sometimes the existence of pathways seemingly unique to certain species, sometimes selection biases linked to peculiarities of the organisms under investigation.

Kubota Y et al. (2006) Biol Chem "C. elegans as a model system to study the function of the COG complex in animal development."

Nishiwaki K, Kubota Y

[Biol Chem, 2006]

The conserved oligomeric Golgi (COG) complex is an octameric protein complex associated with the Golgi apparatus and is required for proper sorting and glycosylation of Golgi resident enzymes and secreted proteins. Although COG complex function has been extensively studied at the cellular and subcellular levels, its role in animal development mostly remains unknown. Recently, mutations in the components of the COG complex were found to cause abnormal gonad morphogenesis in Caenorhabditis elegans. In C. elegans, the COG complex acts in the glycosylation of an ADAM (a disintegrin and metalloprotease) family protein, MIG-17, which directs migration of gonadal distal tip cells to lead gonad morphogenesis. This is the first link between the COG complex and the function of an ADAM protease that is directly involved in organ morphogenesis, demonstrating the potential of C. elegans as a model system to study COG function in animal development.

Cuasnicu PS et al. (2001) Arch Med Res "Molecular mechanisms involved in mammalian gamete fusion."

Da Ros VG, Cohen DJ, Morgenfeld MM, Busso D, Cuasnicu PS, Ellerman DA

[Arch Med Res, 2001]

Fusion between gametes is a key event in the fertilization process involving the interaction of specific domains of the sperm and egg plasma membranes. During recent years, efforts have been made toward the identification of the specific molecular components involved in this event. The present work will focus on the best characterized candidates for mediating gamete membrane fusion in mammals. These molecules include members of the ADAM (a disintegrin and a metalloprotease domain) family, i.e., testicular proteins fertilin alpha, fertilin beta, and cyritestin, which are thought to interact with integrins in the egg plasma membrane through their disintegrin domains, and a member of the cysteine-rich secretory proteins (CRISP) family, i.e., epididymal protein DE, which participates in an event subsequent to sperm-egg binding and leading to fusion through specific complementary sites localized on the fusogenic area of the egg surface. The identification and characterization of these molecules will contribute not only to a better understanding of the molecular mechanisms underlying mammalian sperm-egg fusion but also to the development of new methods for both fertility regulation and diagnosis and treatment of human infertility.

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?