title: KChIP1 and frequenin modify shal-evoked potassium currents in pyloric neurons in the lobster stomatogastric ganglion.
abstract: The transient potassium current (I(A)) plays an important role in shaping the firing properties of pyloric neurons in the stomatogastric ganglion (STG) of the spiny lobster, Panulirus interruptus. The shal gene encodes I(A) in pyloric neurons. However, when we over-expressed the lobster Shal protein by shal RNA injection into the pyloric dilator (PD) neuron, the increased I(A) had somewhat different properties from the endogenous I(A). The recently cloned K-channel interacting proteins (KChIPs) can modify vertebrate Kv4 channels in cloned cell lines. When we co-expressed hKChIP1 with lobster shal in Xenopus oocytes or lobster PD neurons, they produced A-currents resembling the endogenous I(A) in PD neurons; compared with currents evoked by shal alone, their voltage for half inactivation was depolarized, their kinetics of inactivation were slowed, and their recovery from inactivation was accelerated. We also co-expressed shal in PD neurons with lobster frequenin, which encodes a protein belonging to the same EF-hand family of Ca(2+) sensing proteins as hKChIP. Frequenin also restored most of properties of the shal-evoked currents to those of the endogenous A-currents, but the time course of recovery from inactivation was not corrected. These results suggest that lobster shal proteins normally interact with proteins in the KChIP/frequenin family to produce the transient potassium current in pyloric neurons.
authors.affiliation: Department of Neurobiology and Behavior, Cornell University, Ithaca, New York 14853, USA. yz34@cornell.edu
authors.forename: Y
authors.initials: Y
authors.lastname: Zhang
authors.forename: J N
authors.initials: JN
authors.lastname: MacLean
authors.forename: W F
authors.initials: WF
authors.lastname: An
authors.forename: C C
authors.initials: CC
authors.lastname: Lanning
authors.forename: R M
authors.initials: RM
authors.lastname: Harris-Warrick
mesh_terms: D000818:Animals; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D017952:Ganglia, Invertebrate / Q000166:cytology / Q000502:physiology; D015870:Gene Expression / Q000502:physiology; D051605:Kv Channel-Interacting Proteins; D008564:Membrane Potentials / Q000502:physiology; D008845:Microinjections; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism; D051580:Neuronal Calcium-Sensor Proteins; D009474:Neurons / Q000502:physiology*; D009479:Neuropeptides; D009865:Oocytes / Q000502:physiology; D033521:Palinuridae; D018408:Patch-Clamp Techniques; D011188:Potassium / Q000378:metabolism; D015221:Potassium Channels / Q000235:genetics / Q000378:metabolism*; D024642:Potassium Channels, Voltage-Gated; D011708:Pylorus / Q000294:innervation; D012313:RNA / Q000494:pharmacology; D051672:Shal Potassium Channels; D014981:Xenopus; D029867:Xenopus Proteins
chemical_list: D002135:Calcium-Binding Proteins; D051605:Kv Channel-Interacting Proteins; D009419:Nerve Tissue Proteins; D051580:Neuronal Calcium-Sensor Proteins; D009479:Neuropeptides; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D051672:Shal Potassium Channels; D029867:Xenopus Proteins; C101464:frequenin calcium sensor proteins; D012313:RNA; D011188:Potassium