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The potassium channel subunit KV3.1b is localized to somatic and axonal membranes of specific populations of CNS neurons
Weiser M; Bueno E; Sekirnjak C; Martone ME; Baker H; Hillman D; Chen S; Thornhill W; Ellisman M; Rudy B
Potassium channels play major roles in the regulation of many aspects of neuronal excitability. These channels are particularly well suited for such multiplicity of roles since there is a large diversity of channel types. This diversity contributes to the ability of specific neurons (and possibly different regions of the same neuron) to respond uniquely to a given input. Neuronal integration depends on the local response of spatially segregated inputs to the cell and the communication of these integration centers with the axon. Therefore, the functional implications of a given set of K+ channels varies depending on their precise location on the neuronal surface. Site-specific antibodies were utilized to characterize the distribution of KV3.1b, a subunit of voltage-gated K+ channels in CNS neurons. KV3.1b subunits are expressed in specific neuronal populations of the rat brain, such as cerebellar granule cells, projecting neurons of deep cerebellar nuclei, the substantia nigra pars-reticulata, the globus pallidus, and the ventral thalamus (reticular thalamic nucleus, ventral lateral geniculate and zona incerta). The KV3.1b protein is also present in various neuronal populations involved in the processing of auditory signals, including the inferior colliculus, the nuclei of the lateral lemniscus, the superior olive, and some parts of the cochlear nuclei; as well as in several other neuronal groups in the brainstem (e.g., in the oculomotor nucleus, the pontine nuclei, the reticulotegmental nucleus of the pons, trigeminal and vestibular nuclei, and the reticular formation) and subsets of neurons in the neocortex, the hippocampus and the caudate-putamen shown by double staining to correspond to neurons containing parvalbumin. KV3.1b subunits are localized predominantly in somatic and axonal membranes (particularly in axonal terminal fields) but are much less prominent in dendritic arborizations. This distribution is different than that of other subunits of voltage gated K+ channels and is consistent with a role in the modulation of action potentials. KV3.1b proteins have a cellular and subcellular distribution different than the related KV3.2 subunits which express in Xenopus oocytes currents similar to those expressed by KV3.1b
PMID: 7790912
ISSN: 0270-6474
CID: 6775
Developmental expression of KV3.2, KV3.1 and GIRK K+ channel proteins in the mammalian CNS [Meeting Abstract]
Bueno, E.; Yang, H.; Ponce, A.; Lau, D. H. P.; Chow, A.; Chen, S.; Rameau, G.; Sekirnjak, C.; Martone, M. E.; Ellisman, M.; Hillman, D.; Rudy, B.; Thornhill, W.
BIOSIS:PREV199598484289
ISSN: 0190-5295
CID: 92259
Are K+ channel beta-subunit NAD(P)H-dependent oxidoreductase proteins? [Meeting Abstract]
McCormack, T.; McCormack, K.; Moreno, H.; Rudy, B.
BIOSIS:PREV199598530739
ISSN: 0190-5295
CID: 92550
Conserved cysteine residues in the cytoplasmic trail of the human neurokinin A receptor are involved in receptor desensitization [Meeting Abstract]
Cyr, C. R.; Josiah, S.; Rudy, B.; Devi, L.; Kris, R. M.
BIOSIS:PREV199598529390
ISSN: 0190-5295
CID: 92551
Cloning, expression and distribution of KV4.3, a new mammalian subunit of A-type, low-voltage-activating potassium channels [Meeting Abstract]
Serodio, P.; Vega-Saenz De Miera, E.; Rudy, B.
BIOSIS:PREV199598484288
ISSN: 0190-5295
CID: 92552
Nitric oxide and cGMP modulate a presynaptic K+ channel in vitro [Meeting Abstract]
Moreno, H.; Bueno, E.; Hernandez Cruz, A.; Ponce, A.; Rudy, B.
BIOSIS:PREV199598442944
ISSN: 0190-5295
CID: 92553
Phosphorylation may be required to activate Shaw related K+ channels [Meeting Abstract]
Vega-Saenz De Miera, E.; Moreno, H.; Rudy, B.
BIOSIS:PREV199598442939
ISSN: 0190-5295
CID: 92554
Alternatively Spliced Carboxyl-Termini Determine The Targeting Of KV3.2 Channels In MDCK Cells [Meeting Abstract]
Ponce, A.; Vega-Saenz De Miera, E.; Moreno, H.; Bueno, E.; Aleman, V.; Rudy, B.
BIOSIS:PREV199598441649
ISSN: 0190-5295
CID: 92555
Clustering of six human 11p15 gene homologs within a 500-kb interval of proximal mouse chromosome 7
Stubbs L; Rinchik EM; Goldberg E; Rudy B; Handel MA; Johnson D
Homologs of genes mapping to human chromosome 11p15 are located in three distinct, widely separated regions of mouse chromosome 7 (Mmu7). To date, six genes have been localized to the most proximal HSA11p15/Mmu7 homology region, including Ldh3 (encoding lactate dehydrogenase C), Ldh1 (lactate dehydrogenase A), Myod1 (myogenic differentiation factor-1), Tph (tryptophan hydroxylase), Saa1 (serum amyloid-A-1), and Kcnc1 (encoding a Shaw-type voltage-gated potassium channel). To define the overall size and organization of this region of Mmu7, we have established a long-range physical map including the murine Ldh1, Ldh3, Saa, Tph, Kcnc1, and Myod1 genes. Our results demonstrate that these six genes are physically clustered and are distributed throughout a 500-kb interval located just proximal of the pink-eyed dilution (p) locus. These data, together with recent mapping studies within the related region of HSA11p15, demonstrate that gene content and organization within this proximal homology segment have been highly conserved throughout evolution
PMID: 7698755
ISSN: 0888-7543
CID: 18834
Identification of molecular components of A-type channels activating at subthreshold potentials
Serodio P; Kentros C; Rudy B
1. Xenopus oocytes injected with rat brain mRNA express a transient K+ current similar to the A current that activates transiently near the threshold for Na+ action potential generation (ISA) seen in somatic recordings from neurons. We used hybrid arrest with antisense oligonucleotides to investigate which of the cloned K+ channel proteins might be components of the channels responsible for the ISA expressed from brain mRNA. An oligonucleotide complementary to a sequence common to all known mammalian Shal-related mRNAs [KV4.1, KV4.2, and KV4.3 (the nomenclature of Sh K+ channel genes of Chandy and colleagues was used in this paper)] blocked the expression of the ISA. An oligonucleotide complementary only to the KV4.2 mRNA, the most abundant Shal-related transcript in rat brain RNA preparations, was also quite efficient in arresting the expression of the ISA from brain. These experiments indicate that Shal-related proteins are important components of the channels carrying the ISA expressed in oocytes injected with brain mRNA. However, there are several significant differences between this ISA and the currents expressed in the same oocytes by in vitro transcribed KV4.1 or KV4.2 cRNA. Most of these differences are eliminated if KV4.1 or KV4.2 cRNA is coinjected with brain poly-(A) RNA treated with antisense oligonucleotides which arrest the expression of the ISA, or with a 2-4Kb rat brain poly-(A) RNA fraction which does not express detectable K+ currents under the same recording conditions. These data support the hypothesis that ISA channels such as those expressed from brain mRNA contain Shal proteins that can be modified by proteins encoded in RNAs that by themselves do not express K+ currents
PMID: 7823083
ISSN: 0022-3077
CID: 6748