CaMKII protein phosphorylates eag protein at Thr-787.

Mutants are hypersensitive to paraquat.

In hyperexitable eag Sh mutants the pattern of endogenous Appl expression is altered and the satellite bouton-promoting activity elicited by overexpression of Appl is partially attenuated.

Slob, identified as a protein that binds to the carboxy-terminal domain of slo, co-immunoprecipitates with eag.

Immunoprecipitation experiments reveal Hk can associate with eag α subunits.

eag coexpression with Sh in Xenopus oocytes accelerates the inactivation and slows the recovery from inactivation of the transient Sh current.

Subunits from eag and Sh functionally interact in Xenopus oocytes, most likely as heteromultimeric channels. Site directed mutagenesis indicates the eag carboxyl terminus is crucial for the interaction with Sh.

Mutations in Khc enhance the para and mel and suppress the Sh and eag mutant phenotypes.

eag channels are voltage-dependent, outwardly rectifying and highly selective for K⁺ over Na⁺ ions. In contrast to results published in FBrf0064383, the eag channel electrophysiological properties in Xenopus oocytes reveal (i) no evidence for Ca²⁺ permeation, (ii) a transient component of outward current reflecting channel inactivation, and (iii) non-superimposable Cole-Moore shift similar in magnitude to that reported for rat-EAG. eag currents run down more rapidly than do mouse-EAG currents in excised macropatches. Rundown is reversible by inserting the patch into the interior the oocyte, indicating that a cytosolic factor regulates channel activity or stability.

Fas2 is necessary for the synaptic sprouting induced by increased activity (eag Sh double mutants) or increased cAMP (dnc).

slo⁴ partially suppresses the synaptic transmission defects conferred by eag (eliminates the repetitive firing of motor axons).

There are parallels in the physiological and behavioural phenotypes caused by eag mutations and Rat\CamKII-I. Interactions of eag and Rat\CamKII-I have been investigated at the behavioural, physiological, genetical and biochemical level.

Ion channel mutants alter synaptic activity at the embryonic neuromuscular junction (NMJ). GluRIIA expression in the postsynaptic membrane is reduced by changes in presynaptic electrical activity. The size of the synaptic domain depends on the level of neural activity during embryonic synaptogenesis.

NOTE: Aspects of these conclusions subsequently challenged, see FBrf0090763.

eag expression in Xenopus oocytes generates channels that have properties of both voltage- and ligand-gated channels. The ability to mediate potassium outward and calcium inward currents is dependent on voltage and cAMP, these properties are likely to be important in the modulation of synaptic efficiency in both the central and peripheral nervous system.

In eag,Sh hyperexcitable double mutants nerve/muscle synaptic ultrastructure is dramatically altered. Two types of synaptic vesicle are depleted and a third is altered in appearance, and there are changes in number and appearance of synaptic densities, and multivesicular bodies.

The eag locus provides a subunit common to different K⁺ channels. The role of the eag subunit for modulating channels, as opposed to that of Sh subunits required for gating, selectivity and conductance of the channel, suggests a combinatorial genetic framework for generating diversified K⁺ channels.

Effects of potassium channel blocking drugs on the presynaptic action potential repolarization after electrotonic stimulation was studied. At least four K⁺ currents contribute to repolarization of the nerve terminal.

The product of the eag locus is involved in the function of one or more type of voltage-gated potassium channel.

The eag polypeptide is more closely related to polypeptides of cyclic nucleotide gated cation channels than to those of voltage gated K⁺ channels.

Sequence analysis of eag genomic and cDNA clones suggest that eag encodes a previously unidentified structural component of voltage sensitive potassium channels.

Sequence analysis of eag cDNA reveals that eag encodes a structural component of potassium channels that is related to but is distinct from all identified potassium channel polypeptides.

eag encodes a subunit common to different K⁺ channels, this supports the idea that combinatorial assembly of different polypeptides contributes to the diversity of K⁺ channels.

Sequence and voltage clamp analysis demonstrate that the eag locus encodes a subunit common to different K⁺ channels. Combinatorial assembly of polypeptides from different genes may contribute to potassium channel diversity.

eag mutations interact synergistically with Shaker mutations, i.e., double mutants are severely abnormal both behaviorally and physiologically (Ganetzky and Wu, 1983).