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Cited by 17Fungal and yeast genetics researchIon channel regulation and functionCalcium signaling and nucleotide metabolism

Elongation Factor 3, EF3, Associates with the Calcium Channel Cch1 and Targets Cch1 to the Plasma Membrane in Cryptococcus neoformans

Open access
Liu, Min, Gelli, Angie·2008·Eukaryotic Cell
DOI 10.1128/ec.00116-08PMC PMC2446666
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Abstract

Ca 2+-mediated signaling events in eukaryotic cells are initiated by Ca 2+channels located in the plasma membranes and endomembranes. Cch1, a high-affinity Ca 2+channel in the plasma membranes of Cryptococcus neoformans and other fungi, plays a role in many different cellular processes, but the mechanisms that regulate Cch1 are not well understood. A Ras recruitment two-hybrid screen was used to identify protein partners of Cch1 as a means of identifying possible mechanisms of channel regulation. Here, we show that Cch1 specifically associates with a cytoplasmic protein known as elongation factor 3 (EF3). The robust interaction between the cytosolic C terminus of the Cch1 protein and EF3 shown here was confirmed by demonstrating that Cch1 could coimmunoprecipitate with EF3 in yeast lysates. To examine the effects of EF3 on Cch1 behavior, we altered the EF3 gene function by constructing a C. neoformans antisense EF3 repression strain. Our results show that the repression of EF3 led to the mislocalization of Cch1, suggesting a role for EF3 in targeting Cch1 to the plasma membrane of C. neoformans. Consistent with this notion, the antisense EF3 repression strain displayed a growth defect under conditions of limited extracellular Ca 2+. Collectively, these results suggest that EF3 and Cch1 are functionally coupled and that EF3 has a function apart from its role in the protein translation cycle.

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Crossref · 10.1128/ec.00116-08

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  • C. neoformans survival in low extracellular Ca2+ environments depends on the combined activity of Cch1 and Mid1.

    “Its ability to survive in low [Ca 2ϩ ] environments is dependent on the combined activity of Cch1, the predicted pore of the channel complex, and Mid1, a binding partner of Cch1 (7,14,20).”

    From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [14]

  • Cch1 is the only high affinity Ca2+ channel in the plasma membrane of C. neoformans.

    “Genetic analysis has indicated that strains of C. neoformans lacking CCH1 or MID1 were not viable in conditions of limiting extracellular [Ca 2ϩ ], consistent with its role as the only high affinity Ca 2ϩ channel in the plasma membrane (7,14).”

    From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [14]

  • Strains of C. neoformans lacking CCH1 or MID1 were not viable in conditions of limiting extracellular Ca2+.

    “Genetic analysis has indicated that strains of C. neoformans lacking CCH1 or MID1 were not viable in conditions of limiting extracellular [Ca 2ϩ ], consistent with its role as the only high affinity Ca 2ϩ channel in the plasma membrane (7,14).”

    From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [14]

  • Cch1-mediated store depletion-activated Ca2+ currents require co-expression of Cch1 and Mid1, i.e., Cch1 activity requires Mid1.

    “Store depletion-mediated inward Ca 2ϩ currents were not detected in HEK cells that expressed either Cch1 or Mid1 alone or an empty plasmid, indicating that the activation of these Ca 2ϩ currents was completely dependent on the co-expression of Cch1 and Mid1 and that Cch1 activity required Mid1, consistent with previous genetic evidence (Fig. 2, F-H) (12,14,20,21).”

    From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [14]

  • Recent evidence demonstrated that localization of Cch1 to the plasma membrane in cryptococcal cells is dependent on elongation factor EF3, suggesting Mid1 is excluded from this process.

    “In addition, recent evidence has demonstrated that the localization of Cch1 to the plasma membrane in cryptococcal cells is dependent on an elongation factor (EF3), further suggesting that Mid1 is excluded from this process (14).”

    From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [14]

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Authors
Liu, M., & Gelli, A.
Affiliations
  • Santa Clara Valley Medical Center (US)
  • University of California, Davis (US)
Corresponding author
Gelli, Angie
ORCID
Venue
Eukaryotic Cell
Publisher
American Society for Microbiology
Published
2008-07
Volume
7
Issue
7
Pages
1118-1126
ISSN
  • 1535-9778 (ISSN-L)
  • 1535-9786
DOI
10.1128/ec.00116-08
PMC
PMC2446666
OpenAlex
W2166107031
Cited by
15
References
56
Citations by year
2021: 1 · 2016: 1 · 2015: 1 · 2014: 3 · 2012: 4
FWCI
0.68
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Eukaryotic Cell (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
calcium channels, Cryptococcus neoformans, plasma membrane targeting, protein-protein interaction, calcium signaling, protein mislocalization
MeSH terms
Amino Acid Sequence, Cell Membrane, Cryptococcus neoformans, Fungal Proteins, Molecular Sequence Data, Peptide Elongation Factors, Protein Binding, Transcription, Genetic, Calcium Channels, Oncogene Protein p21(ras), Gene Expression Regulation, Fungal, Sequence Alignment, Two-Hybrid System Techniques, Protein Transport, Immunoprecipitation

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