Yeast has a homologue of mammalian voltage-gated Ca²⁺ channels (VGCCs), enabling the efficient uptake of Ca²⁺ . It comprises two indispensable subunits, Cch1 and Mid1, equivalent to the mammalian pore-forming α₁ and auxiliary α₂ /δ subunits, respectively. Unlike the physiological roles of Cch1/Mid1 channels, the regulatory mechanisms of the yeast VGCC homologue remain unclear. Therefore, we screened candidate proteins that interact with Mid1 by an unbiased proteomic approach and identified a plasma membrane H⁺ -ATPase, Pma1, as a candidate. Mid1 coimmunoprecipitated with Pma1, and Mid1-EGFP colocalized with Pma1-mCherry at the plasma membrane. The physiological relevance of their interaction was determined using the temperature-sensitive mutant, pma1-10. At the nonpermissive temperature, the membrane potential was less negative and Ca²⁺ uptake was lower in pma1-10 than in wild-type cells. Increased extracellular H⁺ increased the rate of Ca²⁺ uptake. Therefore, H⁺ extrusion by Pma1 may be important for Ca²⁺ influx through Cch1/Mid1. These results suggest that Pma1 interacts physically with Cch1/Mid1 Ca²⁺ channels to enhance their activity via its H⁺ -pumping activity.

• PMID: 27935186
• DOI full text
• PubMed
• PubTator

Reference Type

Journal Article

Authors

Cho T, Ishii-Kato A, Fukata Y, Nakayama Y, Iida K, Fukata M, Iida H

Primary Lit For

Additional Lit For

Review For