Structurally and Functionally Conserved Domains in the Diverse Hydrophilic Carboxy-Terminal Halves of Various Yeast and Fungal Na+/H+ Antiporters (Nhalp)

Kamauchi, Shinya; Mitsui, Keiji; Ujike, Satoshi; Haga, Megumi; Nakamura, Norihiro; Inoue, Hiroki; Sakajo, Shigeru; Ueda, Mitsuyoshi; Tanaka, Atsuo; Kanazawa, Hiroshi

doi:10.1093/oxfordjournals.jbchem.a003171

Cited by 34 publications

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“…We have also shown that these conserved domains probably play similar functions in yeast and other fungi (28). The C1, C2, and C3 domains consist of 16,23, and 15 residues, respectively, and are located at the juxtamembrane area of the cytoplasmic tail region.…”

Section: Namentioning

confidence: 73%

“…Although the overall primary sequences of the cytoplasmic tail regions of the various Nha1p proteins vary among various yeast species, we have reported that this region bears six small but distinct conserved domains that we have denoted C1 to C6 (28). We have also shown that these conserved domains probably play similar functions in yeast and other fungi (28).…”

Section: Namentioning

confidence: 90%

“…The yeast Na ϩ /H ϩ antiporter SOD2 in Schizosaccharomyces pombe was originally discovered as a factor that makes the cell growth resistant to high NaCl levels in the medium (11). The SOD2 isoform denoted as NHA1 also exists in other yeasts (26 -28) and fungal species (28), including Saccharomyces cerevisiae (29), and it has been shown to antiport Na ϩ for H ϩ (30,31). As with the mammalian NHE family, the Nha1p family of proteins bear a highly conserved integral membrane region and a structurally diverse cytoplasmic tail region (28).…”

Section: Namentioning

confidence: 99%

“…The SOD2 isoform denoted as NHA1 also exists in other yeasts (26 -28) and fungal species (28), including Saccharomyces cerevisiae (29), and it has been shown to antiport Na ϩ for H ϩ (30,31). As with the mammalian NHE family, the Nha1p family of proteins bear a highly conserved integral membrane region and a structurally diverse cytoplasmic tail region (28). Nha1p-mediated export of Na ϩ is coupled to the proton motive force created by the H ϩ -translocating ATPase on the cytoplasmic membrane (31).…”

Section: Namentioning

confidence: 99%

“…The C1, C2, and C3 domains consist of 16,23, and 15 residues, respectively, and are located at the juxtamembrane area of the cytoplasmic tail region. Deletion of these domains decreases salinity-resistant growth, which suggests that these domains are important for growth during highly saline conditions, possibly because they influence the antiporter activity of Nha1p (28). However, the precise mechanisms by which these domains confer salinity resistance have not yet been clarified.…”

Section: Namentioning

confidence: 99%

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A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

Mitsui

Ochi

Nakamura

et al. 2004

Journal of Biological Chemistry

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The Na؉ /H ؉ antiporter Nha1p of Saccharomyces cerevisiae plays an important role in maintaining intracellular pH and Na ؉ homeostasis. Nha1p has a two-domain structure composed of integral membrane and hydrophilic tail regions. Overexpression of a peptide of ϳ40 residues (C1؉C2 domains) that is localized in the juxtamembrane area of its cytoplasmic tail caused cell growth retardation in highly saline conditions, possibly by decreasing Na ؉ /H ؉ antiporter activity. A multicopy suppressor gene of this growth retardation was identified from a yeast genome library. The clone encodes a novel membrane protein denoted as COS3 in the genome data base. Overexpression or deletion of COS3 increases or decreases salinity-resistant cell growth, respectively. However, in nha1⌬ cells, overexpression of COS3 alone did not suppress the growth retardation. Cos3p and a hydrophilic portion of Cos3p interact with the C1؉C2 peptide in vitro, and Cos3p is co-precipitated with Nha1p from yeast cell extracts. Cos3p-GFP mainly resides at the vacuole, but overexpression of Nha1p caused a portion of the Cos3p-GFP proteins to shift to the cytoplasmic membrane. These observations suggest that Cos3p is a novel membrane protein that can enhance salinity-resistant cell growth by interacting with the C1؉C2 domain of Nha1p and thereby possibly activating the antiporter activity of this protein.

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Section: Namentioning

confidence: 73%

Section: Namentioning

confidence: 90%

Section: Namentioning

confidence: 99%

Section: Namentioning

confidence: 99%

Section: Namentioning

confidence: 99%

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A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

Mitsui

Ochi

Nakamura

et al. 2004

Journal of Biological Chemistry

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Structure and function of yeast and fungal Na⁺/H⁺ antiporters

Dutta

Fliegel

2017

IUBMB Life

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Sodium proton antiporters (or sodium proton exchangers [NHEs]) are a critical family of membrane proteins that exchange sodium for protons across cell membranes. In yeast and plants, their primary function is to keep the sodium concentration low inside the cytoplasm. One class of NHE constitutively expressed in yeast is the plasma membrane Na 1 /H 1 antiporter, and another class is expressed on the endosomal/ vacuolar membrane. At present, four bacterial plasma membrane antiporter structures are known and nuclear magnetic resonance structures are available for the membrane spanning transmembrane helices of mammalian and yeast NHEs.Additionally, a vast amount of mutational data are available on the role of individual amino acids and critical motifs involved in transport. We combine this information to obtain a more detailed picture of the yeast NHE plasma membrane protein and review mechanisms of transport, conserved motifs, unique residues important in function, and regulation of these proteins. The Na

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Monovalent cation transporters at the plasma membrane in yeasts

Ariño

Ramos

Sychrová

2018

Yeast

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Maintenance of proper intracellular concentrations of monovalent cations, mainly sodium and potassium, is a requirement for survival of any cell. In the budding yeast Saccharomyces cerevisiae, monovalent cation homeostasis is determined by the active extrusion of protons through the Pma1 H -ATPase (reviewed in another chapter of this issue), the influx and efflux of these cations through the plasma membrane transporters (reviewed in this chapter), and the sequestration of toxic cations into the vacuoles. Here, we will describe the structure, function, and regulation of the plasma membrane transporters Trk1, Trk2, Tok1, Nha1, and Ena1, which play a key role in maintaining physiological intracellular concentrations of Na , K , and H , both under normal growth conditions and in response to stress.

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Structurally and Functionally Conserved Domains in the Diverse Hydrophilic Carboxy-Terminal Halves of Various Yeast and Fungal Na+/H+ Antiporters (Nhalp)

Cited by 34 publications

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A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

Structure and function of yeast and fungal Na⁺/H⁺ antiporters

Monovalent cation transporters at the plasma membrane in yeasts

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Structurally and Functionally Conserved Domains in the Diverse Hydrophilic Carboxy-Terminal Halves of Various Yeast and Fungal Na+/H+ Antiporters (Nhalp)

Cited by 34 publications

References 0 publications

A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

A Novel Membrane Protein Capable of Binding the Na+/H+ Antiporter (Nha1p) Enhances the Salinity-resistant Cell Growth of Saccharomyces cerevisiae

Structure and function of yeast and fungal Na+/H+ antiporters

Monovalent cation transporters at the plasma membrane in yeasts

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Product

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Structure and function of yeast and fungal Na⁺/H⁺ antiporters