{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T06:32:18Z","timestamp":1791095538871,"version":"4.1.0"},"reference-count":51,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The Saccharomyces casein kinase 1 isoforms encoded by the essential gene pair YCK1 and YCK2 control cell growth and morphogenesis and are linked to the endocytosis of several membrane proteins. Here we define roles for the Yck1,2 kinases in Mal61p maltose permease activation and trafficking, using a yck1\u0394 yck2-2ts (yckts) strain with conditional Yck activity. Moreover, we provide evidence that Glc7\u2013Reg1 phosphatase acts as an upstream activator of Yck1,2 kinases in a novel signaling pathway that modulates kinase activity in response to carbon source availability. The yckts strain exhibits significantly reduced maltose transport activity despite apparently normal levels and cell surface localization of maltose permease protein. Glucose-induced internalization and rapid loss of maltose transport activity of Mal61\/HAp-GFP are not observed in the yckts strain and maltose permease proteolysis is blocked. We show that a reg1\u0394 mutant exhibits a phenotype remarkably similar to that conferred by yckts. The reg1\u0394 phenotype is not enhanced in the yckts reg1\u0394 double mutant and is suppressed by increased Yck1,2p dosage. Further, although Yck2p localization and abundance do not change in the reg1\u0394 mutant, Yck1,2 kinase activity, as assayed by glucose-induced HXT1 expression and Mth1 repressor stability, is substantially reduced in the reg1\u0394 strain.<\/jats:p>","DOI":"10.1534\/genetics.105.051698","type":"journal-article","created":{"date-parts":[[2005,12,19]],"date-time":"2005-12-19T13:02:45Z","timestamp":1134997365000},"page":"1427-1439","source":"Crossref","is-referenced-by-count":43,"title":["Glc7\u2013Reg1 Phosphatase Signals to Yck1,2 Casein Kinase 1 to Regulate Transport Activity and Glucose-Induced Inactivation of Saccharomyces Maltose Permease"],"prefix":"10.1093","volume":"172","author":[{"given":"Nidhi","family":"Gadura","sequence":"first","affiliation":[{"name":"Biology Department, Queens College and the Graduate School of CUNY, Flushing, New York 11367 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucy C","family":"Robinson","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, LSU Health Sciences Center, Shreveport, Louisiana 71130"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Corinne A","family":"Michels","sequence":"additional","affiliation":[{"name":"Biology Department, Queens College and the Graduate School of CUNY, Flushing, New York 11367 and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2006,3,1]]},"reference":[{"key":"2022010800213731300_BIB1","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S1534-5807(02)00220-4","volume":"3","year":"2002","journal-title":"Dev. 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