A Homolog of Voltage-Gated Ca<sup>2+</sup>Channels Stimulated by Depletion of Secretory Ca<sup>2+</sup> in Yeast

Locke, Emily; Bonilla, Myriam; Liang, Linda; Takita, Yoko; Cunningham, Kyle W.

doi:10.1128/mcb.20.18.6686-6694.2000

Cited by 208 publications

(274 citation statements)

References 65 publications

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“…In addition, Mid1 functions in an amiodarone-induced increase in cytosolic Ca 2ϩ , whereas Cch1 does not (20). On the other hand, it has been shown that the phenotypes of mid1 and cch1 single mutants and a mid1 cch1 double mutant are essentially the same (10,17,18), and immunoprecipitation experiments have shown that Mid1 coprecipitates with Cch1 (10), suggesting that Mid1 and Cch1 cooperate to work in some conditions. Two possible structure-function relationships could be hypothesized.…”

Section: H3 and H4 May Not Be Required For The Localization Of The MImentioning

confidence: 99%

“…These non-pore-forming subunits dramatically influence the properties and surface expression of the channels (12)(13)(14)(15)(16). Although the channel activity of Cch1 has not yet been revealed experimentally and Mid1 has no homology to the auxiliary subunits, Mid1 has been shown to cooperate with Cch1 in mating pheromone-induced Ca 2ϩ uptake (8,9,17), store-operated or capacitative Ca 2ϩ entry (10), endoplasmic reticulum stress-induced Ca 2ϩ uptake (18), and a hyperosmotic stress-induced increase in cytosolic Ca 2ϩ (19). On the other hand, it has been shown recently that Mid1, but not Cch1, is required for an antiarrhythmic drug amiodarone-induced increase in cytosolic Ca 2ϩ mainly caused by Ca 2ϩ influx (20).…”

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confidence: 99%

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Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Tada¹,

Ohmori²,

Iida³

2003

Journal of Biological Chemistry

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The Saccharomyces cerevisiae MID1 gene product, Mid1, is composed of 548 amino acid residues, has four relatively hydrophobic segments named H1-H4, and functions as a Ca 2؉ -permeable, stretch-activated channel when expressed in mammalian cells. In some conditions Mid1 cooperates with Cch1, a yeast homolog of the ␣1 subunit of mammalian voltage-gated channels. To identify the important regions or amino acid residues necessary for Mid1 function, we employed in vitro sitedirected mutagenesis on H3 and H4 of Mid1 and expressed the resulting mutant genes in a mid1 null mutant to examine whether the mutant gene products are functional or not in vivo. Mutant Mid1 proteins lacking the whole H3 or H4 segment, H3De or H4De, did not complement the lethality and low Ca 2؉ accumulation activity of the mid1 mutant, although their localization and contents appeared to be normal, indicating that H3 and H4 are required for Mid1 function itself. Single amino acid exchange experiments on individual amino acid residues of H3 and H4 showed that 10 of 20 residues in H3 and 14 of 23 residues in H4 were important for the normal function of Mid1. In particular, we found four severe loss-of-function mutations, D341E, F356S, C373D, and C373R, and two interesting mutations leading to a high level of Ca 2؉ accumulation with a slightly low complementing activity, G342A and Y355A. The importance of these amino acid residues will be discussed.

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Section: H3 and H4 May Not Be Required For The Localization Of The MImentioning

confidence: 99%

mentioning

confidence: 99%

Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Tada¹,

Ohmori²,

Iida³

2003

Journal of Biological Chemistry

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“…Cellular calcium levels in S. cerevisiae are regulated by multiple channels and transporters, including the voltage-gated high-affinity calcium channel Cch1 which functions together with the stretch-activated cation channel Mid1 (Locke et al, 2000). In contrast to the transmembrane protein Cch1, Mid1 is anchored to the membrane by a GPI-anchor.…”

Section: The Calcium/calcineurin Signalling Pathwaymentioning

confidence: 99%

Comparative genomics of MAP kinase and calcium–calcineurin signalling components in plant and human pathogenic fungi

Rispail

Soanes

Ant

et al. 2009

Fungal Genetics and Biology

285

281

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a b s t r a c tMitogen-activated protein kinase (MAPK) cascades and the calcium-calcineurin pathway control fundamental aspects of fungal growth, development and reproduction. Core elements of these signalling pathways are required for virulence in a wide array of fungal pathogens of plants and mammals. In this review, we have used the available genome databases to explore the structural conservation of three MAPK cascades and the calcium-calcineurin pathway in ten different fungal species, including model organisms, plant pathogens and human pathogens. While most known pathway components from the model yeast Saccharomyces cerevisiae appear to be widely conserved among taxonomically and biologically diverse fungi, some of them were found to be restricted to the Saccharomycotina. The presence of multiple paralogues in certain species such as the zygomycete Rhizopus oryzae and the incorporation of new functional domains that are lacking in S. cerevisiae signalling proteins, most likely reflect functional diversification or adaptation as filamentous fungi have evolved to occupy distinct ecological niches.

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“…However, these proteins can still respond to some stimuli differently, suggesting common but also individual functions of the two channels (24,50). Recently, it has been shown by a yeast two-hybrid approach that these proteins also interact in A. nidulans (55).…”

Section: Discussionmentioning

confidence: 99%

“…In yeast, Cch1 is localized in the plasma membrane, where it forms a complex with Mid1. Both proteins have been shown to be required for the uptake of extracellular Ca 2ϩ in cells responding to mating pheromones (13,(21)(22)(23)(24).…”

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confidence: 99%

Cch1 and Mid1 Are Functionally Required for Vegetative Growth under Low-Calcium Conditions in the Phytopathogenic Ascomycete Botrytis cinerea

Harren

Tudzynski

2013

Eukaryot Cell

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In the filamentous phytopathogen Botrytis cinerea, the Ca 2؉ /calcineurin signaling cascade has been shown to play an important role in fungal growth, differentiation, and virulence. This study deals with the functional characterization of two components of this pathway, the putative calcium channel proteins Cch1 and Mid1. The cch1 and mid1 genes were deleted, and single and double knockout mutants were analyzed during different stages of the fungal life cycle. Our data indicate that Cch1 and Mid1 are functionally required for vegetative growth under conditions of low extracellular calcium, since the growth of both deletion mutants is strongly impaired when they are exposed to the Ca 2؉ -chelating agents EGTA and 1,2-bis(o-aminophenoxy)ethane-N,N,N=,N=-tetraacetic acid (BAPTA). The impact of external Ca 2؉ was investigated by supplementing with CaCl 2 and the ionophore A23187, both of which resulted in elevated growth for all mutants. However, deletion of either gene had no impact on germination, sporulation, hyphal morphology, or virulence. By use of the aequorin reporter system to measure intracellular calcium levels, no differences between the mutant strains and the wild type were obtained. Localization studies revealed a subcellular distribution of the Mid1-green fluorescent protein (GFP) fusion protein in network-like filaments, probably the endoplasmic reticulum (ER) membranes, indicating that Mid1 is not a plasma membrane-located calcium channel in B. cinerea.

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A Homolog of Voltage-Gated Ca²⁺Channels Stimulated by Depletion of Secretory Ca²⁺ in Yeast

Cited by 208 publications

References 65 publications

Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Comparative genomics of MAP kinase and calcium–calcineurin signalling components in plant and human pathogenic fungi

Cch1 and Mid1 Are Functionally Required for Vegetative Growth under Low-Calcium Conditions in the Phytopathogenic Ascomycete Botrytis cinerea

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A Homolog of Voltage-Gated Ca2+Channels Stimulated by Depletion of Secretory Ca2+ in Yeast

Cited by 208 publications

References 65 publications

Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1

Comparative genomics of MAP kinase and calcium–calcineurin signalling components in plant and human pathogenic fungi

Cch1 and Mid1 Are Functionally Required for Vegetative Growth under Low-Calcium Conditions in the Phytopathogenic Ascomycete Botrytis cinerea

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A Homolog of Voltage-Gated Ca²⁺Channels Stimulated by Depletion of Secretory Ca²⁺ in Yeast