Luo S et al. (2006) J Biol "Regulators of kinesin involved in polarized trafficking and axon outgrowth."

Nonet ML, Luo S

[J Biol, 2006]

ABSTRACT : Proteins such as UNC-76 that associate with kinesin motors are important in directing neurite extension. A small Caenorhabditis elegans coiled-coil protein, UNC-69, has now been shown to interact with UNC-76 and to be involved in axonal (but not dendritic) transport and outgrowth, as well as synapse formation.

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."

Nurrish SJ, Lackner MR, 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

Ch'ng Q (2011) BMC Biol "Selecting synaptic partners: GRASPing the role of UNC-6/netrin."

Ch'ng Q

[BMC Biol, 2011]

Forming synaptic connections of the appropriate strength between specific neurons is crucial for constructing neural circuits to control behavior. A recent paper in Neural Development describes the use of a synapse-specific label in Caenorhabditis elegans to implicate local UNC-6/netrin signaling in this developmental process. Thus, as well as their well known roles in cell migration and axon guidance, UNC-6/netrin signals distinguish an appropriate synaptic partner from other potential targets.

Gonczy P (2004) Cell "Myosin assembly: the power of multiubiquitylation."

Gonczy P

[Cell, 2004]

Ubiquitylation provides a means of targeting substrate proteins for degradation by the proteasome. Novel findings in C. elegans (Hoppe et al., 2004, this issue of Cell) establish that two ubiquitin-ligases team up to multiubiquitylate the myosin chaperone UNC-45, suggesting a novel link between regulated protein degradation and myosin assembly.

Corey DP et al. (1996) Science "Mechanosensation and the DEG/ENaC ion channels."

Garcia-Anoveros J, Corey DP

[Science, 1996]

Mechanosensation -the transformation of mechanical stimuli into electrochemical signals-is ubiquitous in animals; it includes the senses of hearing, balance, touch, proprioception, as well as cellular functions such as volume regulation. The molecular basis of mechanosensitivity has been hard to discern because mechanosensitive organs are small and their constituent proteins are scarce. Recent genetic studies in the nematode Caenorhabditis elegans have revealed a dozen candidate proteins for mediating the sense of touch, in the process defining a new superfamily of ion channel proteins. A report in this issue now describes two interacting genes (unc-105 and let-2) expressed by C. elegans muscle that may be involved in the muscle's response to stretch; unc-105 is a new member of this channel superfamily and let-2 encodes a collagen.

Nonet ML (2002) Neuron "AEXpulsing a retrograde signal."

Nonet ML

[Neuron, 2002]

A variety of secreted components have been identified as retrograde signals mediating diverse aspects of synaptic development, maintenance, and plasticity; however, little is known about the mechanisms mediating the release of secreted retrograde signals. Doi and Iwasaki (this issue of Neuron) implicate AEX-1, a protein distantly related to the UNC-13/Munc13 family, as an attractive candidate regulator of the retrograde release machinery in muscle.