Behavioral adaptation of the Aplysia siphon-withdrawal response is accompanied by sensory adaptation

Calin-Jageman RJ, Fischer TM

Behav. Neurosci. 2007 Feb;121(1):200-11

PMID: 17324064


Behavioral adaptation is a decrease in behavioral responsiveness due to a sustained stimulus and is a key component to an organism’s overall adjustment to its ambient environment. The authors examined the relationship between behavioral adaptation and sensory adaptation in the siphon-withdrawal reflex (SWR) of Aplysia californica. Sensory input to the SWR circuit was measured via en passant extracellular recordings from the siphon nerve in semi-intact preparations. The authors characterized sensory activity in response to water turbulence, an ethologically relevant stimulus that produces behavioral adaptation of the SWR. The authors found that water turbulence elicits a continuous sensory response that adapts to a low-level steady state. Consistent with behavioral measures, this sensory adaptation attenuates the evoked response to siphon taps delivered during water turbulence. Comparing trends in both behavioral and sensory adaptation revealed similar dynamics during turbulence but divergent trends during recovery. Specifically, behavioral recovery was inversely related to the duration of environmental change; recovery of sensory adaptation was not. This supports the authors’ hypothesis that environment-driven behavioral adaptation reflects an interaction between sensory adaptation and additional dynamic processes.

Erbin enhances voltage-dependent facilitation of Ca(v)1.3 Ca2+ channels through relief of an autoinhibitory domain in the Ca(v)1.3 alpha1 subunit

Calin-Jageman I, Yu K, Hall RA, Mei L, Lee A

J. Neurosci. 2007 Feb;27(6):1374-85

PMID: 17287512


Ca(v)1.3 (L-type) voltage-gated Ca2+ channels have emerged as key players controlling Ca2+ signals at excitatory synapses. Compared with the more widely expressed Ca(v)1.2 L-type channel, relatively little is known about the mechanisms that regulate Ca(v)1.3 channels. Here, we describe a new role for the PSD-95 (postsynaptic density-95)/Discs large/ZO-1 (zona occludens-1) (PDZ) domain-containing protein, erbin, in directly potentiating Ca(v)1.3. Erbin specifically forms a complex with Ca(v)1.3, but not Ca(v)1.2, in transfected cells. The significance of erbin/Ca(v)1.3 interactions is supported by colocalization in somatodendritic domains of cortical neurons in culture and coimmunoprecipitation from rat brain lysates. In electrophysiological recordings, erbin augments facilitation of Ca(v)1.3 currents by a conditioning prepulse, a process known as voltage-dependent facilitation (VDF). This effect requires a direct interaction of the erbin PDZ domain with a PDZ recognition site in the C-terminal domain (CT) of the long variant of the Ca(v)1.3 alpha1 subunit (alpha1 1.3). Compared with Ca(v)1.3, the Ca(v)1.3b splice variant, which lacks a large fraction of the alpha1 1.3 CT, shows robust VDF that is not further affected by erbin. When coexpressed as an independent entity with Ca(v)1.3b or Ca(v)1.3 plus erbin, the alpha1 1.3 CT strongly suppresses VDF, signifying an autoinhibitory function of this part of the channel. These modulatory effects of erbin, but not alpha1 1.3 CT, depend on the identity of the auxiliary Ca2+ channel beta subunit. Our findings reveal a novel mechanism by which PDZ interactions and alternative splicing of alpha1 1.3 may influence activity-dependent regulation of Ca(v)1.3 channels at the synapse.