<i>YKC1</i> encodes the depolarization‐activated K<sup>+</sup> channel in the plasma membrane of yeast

Zhou, Xin; Vaillant, Brian; Loukin, Stephen H.; Kung, Ching; Saimi, Yoshiro

doi:10.1016/0014-5793(95)01035-d

Cited by 93 publications

(91 citation statements)

References 19 publications

(44 reference statements)

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“…In contrast, evidence for heteromultimer formation within, but not among, certain Kv and Kir subfamilies has been documented [2][3][4][5]13,21]. In connection with structural diversity of K + channels, two new classes represented by respectively TOK1 and YKC1 isolated from Saccharomyces cerevisiae, and CeK1,2,3 from the nematode Caenorhabditis elegans, have recently been reported [22][23][24]. It has been proposed that these channels, characterized by the unique feature of two pore domain-containing subunits in tandem, may function as a dimer.…”

Section: Discussionmentioning

confidence: 99%

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

et al. 1996

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Possible heteromultimer formation between Kv-and Kit-type K + channels was investigated, in connection with the known functional diversity of K + channels in vivo. Voltage-clamp experiments were performed on Xenopus oocytes, either injected with concatenated Kir2.1-Kvl.1 mRNA, or co-injected with Kvl.1 and Kir2.1 mRNA. K + currents could be approximated by the algebraic sum of the 2 K + current types alone. The tandem construct did not show functional expression, although it could be detected by Western blotting. We conclude that Kvl.1 and Kir2.1 a-subunit proteins fail to assemble and do not contribute functional diversity to K + channels.

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Section: Discussionmentioning

confidence: 99%

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

et al. 1996

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“…Moreover, there are combinations of voltage-gating modules and pore modules, such as channels made of two 2-TM pore modules (K 2P ) (Goldstein et al, 1996; Lesage et al, 1996; Brohawn et al, 2012), a 6-TM domain and two 2-TM pore module found in fungi (TOK1) (Ketchum et al, 1995;Zhou et al, 1995), as well as two 6-TM domains (TPC) (Ishibashi et al, 2000).…”

Section: Reviewmentioning

confidence: 99%

Evolution of voltage-gated ion channels at the emergence of Metazoa

Moran

Barzilai

Liebeskind

et al. 2015

Journal of Experimental Biology

128

116

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Voltage-gated ion channels are large transmembrane proteins that enable the passage of ions through their pore across the cell membrane. These channels belong to one superfamily and carry pivotal roles such as the propagation of neuronal and muscular action potentials and the promotion of neurotransmitter secretion in synapses. In this review, we describe in detail the current state of knowledge regarding the evolution of these channels with a special emphasis on the metazoan lineage. We highlight the contribution of the genomic revolution to the understanding of ion channel evolution and for revealing that these channels appeared long before the appearance of the first animal. We also explain how the elucidation of channel selectivity properties and function in non-bilaterian animals such as cnidarians (sea anemones, corals, jellyfish and hydroids) can contribute to the study of channel evolution. Finally, we point to open questions and future directions in this field of research. KEY WORDS: Voltage-gated ion channels, Animal evolution, Ion selectivity Introduction: the superfamily of voltage-gated ion channelsThis review aims to cover and clarify the evolution and diversification of metazoan voltage-gated ion channels, particularly at the beginning of multicellularity in the lineage leading to Metazoa and at the emergence of nervous systems. Voltage-gated ion channels are imperative for neuronal signaling, muscle contraction and secretion, and are thought to play a critical role in the evolution of animals (Hille, 2001). Nonetheless, these channels are also found in prokaryotes and viruses, although their roles in these organisms are largely unknown (Martinac et al., 2008;Plugge et al., 2000). The superfamily of voltage-gated ion channels is characterized by the ability to rapidly respond to changes in membrane potential (hence 'voltage-gated'), which results in selective ion conductance. This ion channel superfamily includes voltage-gated potassium channels (K V s), voltage-gated calcium channels (Ca V s) and voltage-gated sodium channels (Na V s). Their α-subunits are composed of four domains (DI-IV), with each domain containing six transmembrane segments (S1-S6; Fig. 1) (Noda et al., 1984;Noda et al., 1986;Guy and Seetharamulu, 1986;Tanabe et al., 1987). Voltage-dependent activation is enabled by conserved positively charged residues at every third position in S4 (voltage sensor) of the four domains, which move outwards upon changes in membrane potential (Noda et al., 1984; Catterall, 1986;Guy and Seetharamulu, 1986), inducing a conformational change that results in opening of the channel pore (Armstrong and Bezanilla, 1974;Stühmer et al., 1989;Papazian et al., 1991;Yang et al., 1996). The pore is formed by the segments S5 and S6, and the selectivity to specific ions is enabled by the selectivity filter, which is composed of conserved residues, specific for the ion conducted by the channel, and these residues are situated at the pore-lining loops (p-loops) connecting S5 to S6 in the four domains ( ...

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“…We have recently succeeded in whole cell patch clamp recordings of the yeast giant protoplasts as well. Thus, a combination of these two methods together shall provide a powerful system for analyzing any ion transporter, not only highly active channels (5)(6)(7)(8)(9)(10)(11)(12)(45)(46)(47)(48) but also other weaker transporters in the membranes, either vacuolar or cytoplasmic, of S. cerevisiae. We used haploid cells because they are much easier than polyploid ones to manipulate genes to yield deletion mutants.…”

Section: H ϩ -Pump Current Of V-type Atpase In Yeast Giant Vacuolesmentioning

confidence: 99%

Patch Clamp Studies on V-type ATPase of Vacuolar Membrane of Haploid Saccharomyces cerevisiae

Yabe¹,

Horiuchi²,

Nakahara³

et al. 1999

Journal of Biological Chemistry

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Complete inhibition at higher concentrations indicated that any other ATP-driven transport systems were not expressed under the present incubation conditions. This current was not observed in the vacuoles prepared from a mutant that disrupted a catalytic subunit of the V-type ATPase (RH105(⌬vma1::TRP)). The K m value for the ATP dose response of the current was 159 M and the H ؉ /ATP ratio estimated from the reversible potential of the V-I curve was 3.5 ؎ 0.3. These values agreed well with those previously estimated by measuring the V-type ATPase activity biochemically. This method can potentially be applied to any type of ion channel, ion pump, and ion transporter in S. cerevisiae, and can also be used to investigate gene functions in various organisms by using yeast cells as hosts for homologous and heterogeneous expression systems.

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YKC1 encodes the depolarization‐activated K⁺ channel in the plasma membrane of yeast

Cited by 93 publications

References 19 publications

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

Evolution of voltage-gated ion channels at the emergence of Metazoa

Patch Clamp Studies on V-type ATPase of Vacuolar Membrane of Haploid Saccharomyces cerevisiae

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YKC1 encodes the depolarization‐activated K+ channel in the plasma membrane of yeast

Cited by 93 publications

References 19 publications

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

Do voltage‐gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

Evolution of voltage-gated ion channels at the emergence of Metazoa

Patch Clamp Studies on V-type ATPase of Vacuolar Membrane of Haploid Saccharomyces cerevisiae

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YKC1 encodes the depolarization‐activated K⁺ channel in the plasma membrane of yeast