{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T06:27:40Z","timestamp":1783751260411,"version":"3.55.0"},"reference-count":76,"publisher":"The Company of Biologists","issue":"16","license":[{"start":{"date-parts":[[2012,2,15]],"date-time":"2012-02-15T00:00:00Z","timestamp":1329264000000},"content-version":"vor","delay-in-days":184,"URL":"http:\/\/www.biologists.com\/user-licence-1-1"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,8,15]]},"abstract":"<jats:p>Intracellular Ca2+ signals influence gastrulation, neurogenesis and organogenesis through pathways that are still being defined. One potential Ca2+ mediator of many of these morphogenic processes is CaMK-II, a conserved calmodulin-dependent protein kinase. Prolonged Ca2+ stimulation converts CaMK-II into an activated state that, in the zebrafish, is detected in the forebrain, ear and kidney. Autosomal dominant polycystic kidney disease has been linked to mutations in the Ca2+-conducting TRP family member PKD2, the suppression of which in vertebrate model organisms results in kidney cysts. Both PKD2-deficient and CaMK-II-deficient zebrafish embryos fail to form pronephric ducts properly, and exhibit anterior cysts and destabilized cloacal cilia. PKD2 suppression inactivates CaMK-II in pronephric cells and cilia, whereas constitutively active CaMK-II restores pronephric duct formation in pkd2 morphants. PKD2 and CaMK-II deficiencies are synergistic, supporting their existence in the same genetic pathway. We conclude that CaMK-II is a crucial effector of PKD2 Ca2+ that both promotes morphogenesis of the pronephric kidney and stabilizes primary cloacal cilia.<\/jats:p>","DOI":"10.1242\/dev.066340","type":"journal-article","created":{"date-parts":[[2011,7,14]],"date-time":"2011-07-14T02:17:38Z","timestamp":1310609858000},"page":"3387-3397","source":"Crossref","is-referenced-by-count":36,"title":["CaMK-II is a PKD2 target that promotes pronephric kidney development and stabilizes cilia"],"prefix":"10.1242","volume":"138","author":[{"given":"Sarah C.","family":"Rothschild","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ludmila","family":"Francescatto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iain A.","family":"Drummond","sequence":"additional","affiliation":[{"name":"Nephrology Division, Massachusetts General Hospital, Charlestown, MA 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert M.","family":"Tombes","sequence":"additional","affiliation":[{"name":"Department of Biology, Virginia Commonwealth University, Richmond, VA 23284-2012, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042606580692400_R1","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1128\/MCB.01611-07","article-title":"Histone deacetylase 4 confers CaM kinase II responsiveness to histone deacetylase 5 by oligomerization","volume":"28","author":"Backs","year":"2008","journal-title":"Mol. 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