Hodgkin J (2002) Genes Dev "The remarkable ubiquity of DM domain factors as regulators of sexual phenotype: ancestry or aptitude?"

Hodgkin J

[Genes Dev, 2002]

The CM domain is a cysteine-rich DNA-binding motif first recognized in proteins encoded by the Drosophila set determination gene doublesex (Erdman and Burtis 1993; Zhu et al. 2000). As the name doublesex (dsx) suggests, this gene has functions in both sexes: Its transcripts undergo sex-specific alternative splicing, so that it can encode either a male-specific isoform, DSX(M), or a female-specific isoform, DSX(F) (Baker and Wolfner 1988; Burtis and Baker 1989). These proteins have the same N-terminal DNA-binding domain, but different C termini that confer different regulatory properties on the two forms. The expression of DSX(M) directs male development, and the expression of DSX(F) directs female development, throughout most of the somatic tissues of the fruit fly.

Schnabel R et al. (1997) Nature "Hox genes misled by local environments."

Schnabel R, Schnabel H

[Nature, 1997]

Cowing and Kenyon raise an important issue concerning Hox genes by suggesting that these genes may not only be expressed according to position but also according to cell lineage. This suggestion is based on two experiments in which the so-called M cell and two hypodermal V6 cells were manipulated to express a Hox gene, mab-5, outside the posterior region of the Caenorhabditis elegans embryo. Here we propose a less radical interpretation of these data.

Lackner MR et al. (1999) Neuron "Facilitation of synaptic transmission by EGL-30 Gqalpha and EGL-8 PLCbeta: DAG binding to UNC-13 is required to stimulate acetylcholine release."

Lackner MR, Nurrish SJ, Kaplan JM

[Neuron, 1999]

We show that neurotransmitter release at Caenorhabditis elegans neuromuscular junctions is facilitated by a presynaptic pathway composed of a Gqalpha (EGL-30), EGL-8 phospholipase Cbeta (PLCbeta), and the diacylglycerol- (DAG-) binding protein UNC-13. Activation of this pathway increased release of acetylcholine at neuromuscular junctions, whereas inactivation decreased release. Phorbol esters stimulated acetylcholine release, and this effect was blocked by a mutation that eliminates phorbol ester binding to UNC-13. Expression of a constitutively membrane-bound form of UNC-13 restored acetylcholine release to mutants lacking the egl-8 PLCbeta. Activation of this pathway with muscarinic agonists caused UNC-13 to accumulate in punctate structures in the ventral nerve cord. These results suggest that presynaptic DAG facilitates synaptic transmission and that part of this effect is mediated by UNC-13.AD - Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.FAU - Lackner, M RAU - Lackner MRFAU - Nurrish, S JAU - Nurrish SJFAU - Kaplan, J MAU - Kaplan JMLA - engID - GM54728/GM/NIGMSPT - Journal ArticleCY - UNITED STATESTA - NeuronJID - 8809320RN - 0 (Diglycerides)RN - 0 (Helminth Proteins)RN - 0 (Isoenzymes)RN - 0 (Muscarinic Agonists)RN - 0 (Unc-13 protein)RN - 16561-29-8 (Tetradecanoylphorbol Acetate)RN - 51-84-3 (Acetylcholine)RN - EC 3.1.4.- (phospholipase C beta)RN - EC 3.1.4.3 (Phospholipase C)RN - EC 3.6.1.- (GTP-Binding Proteins)SB - IM