{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,19]],"date-time":"2026-05-19T17:32:34Z","timestamp":1779211954678,"version":"3.51.4"},"reference-count":40,"publisher":"Rockefeller University Press","issue":"1","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2002,1,7]]},"abstract":"<jats:p>Calcium ions, present inside all eukaryotic cells, are important second messengers in the transduction of biological signals. In mammalian cells, the release of Ca2+ from intracellular compartments is required for signaling and involves the regulated opening of ryanodine and inositol-1,4,5-trisphosphate (IP3) receptors. However, in budding yeast, no signaling pathway has been shown to involve Ca2+ release from internal stores, and no homologues of ryanodine or IP3 receptors exist in the genome. Here we show that hyperosmotic shock provokes a transient increase in cytosolic Ca2+ in vivo. Vacuolar Ca2+, which is the major intracellular Ca2+ store in yeast, is required for this response, whereas extracellular Ca2+ is not. We aimed to identify the channel responsible for this regulated vacuolar Ca2+ release. Here we report that Yvc1p, a vacuolar membrane protein with homology to transient receptor potential (TRP) channels, mediates the hyperosmolarity induced Ca2+ release. After this release, low cytosolic Ca2+ is restored and vacuolar Ca2+ is replenished through the activity of Vcx1p, a Ca2+\/H+ exchanger. These studies reveal a novel mechanism of internal Ca2+ release and establish a new function for TRP channels.<\/jats:p>","DOI":"10.1083\/jcb.200111004","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T12:46:23Z","timestamp":1027687583000},"page":"29-34","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":271,"title":["Internal Ca2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue"],"prefix":"10.1083","volume":"156","author":[{"given":"Vale\u0301rie","family":"Denis","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Stanford University, Stanford, CA 94305"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martha S.","family":"Cyert","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Stanford University, Stanford, CA 94305"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[2002,1,7]]},"reference":[{"key":"2023072213223667500_BIB1","first-page":"4135","volume":"14","year":"1994","journal-title":"Mol. 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