{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T18:28:27Z","timestamp":1773080907029,"version":"3.50.1"},"reference-count":112,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2015,3,16]]},"abstract":"<jats:p>Casein kinase 1\u03b4\/\u03b5 (CK1\u03b4\/\u03b5) and their yeast homologue Hrr25 are essential for cell growth. Further, CK1\u03b4 is overexpressed in several malignancies, and CK1\u03b4 inhibitors have shown promise in several preclinical animal studies. However, the substrates of Hrr25 and CK1\u03b4\/\u03b5 that are necessary for cell growth and survival are unknown. We show that Hrr25 is essential for ribosome assembly, where it phosphorylates the assembly factor Ltv1, which causes its release from nascent 40S subunits and allows subunit maturation. Hrr25 inactivation or expression of a nonphosphorylatable Ltv1 variant blocked Ltv1 release in vitro and in vivo, and prevented entry into the translation-like quality control cycle. Conversely, phosphomimetic Ltv1 variants rescued viability after Hrr25 depletion. Finally, Ltv1 knockdown in human breast cancer cells impaired apoptosis induced by CK1\u03b4\/\u03b5 inhibitors, establishing that the antiproliferative activity of these inhibitors is due, at least in part, to disruption of ribosome assembly. These findings validate the ribosome assembly pathway as a novel target for the development of anticancer therapeutics.<\/jats:p>","DOI":"10.1083\/jcb.201409056","type":"journal-article","created":{"date-parts":[[2015,3,16]],"date-time":"2015-03-16T15:28:12Z","timestamp":1426519692000},"page":"745-759","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":76,"title":["Hrr25\/CK1\u03b4-directed release of Ltv1 from pre-40S ribosomes is necessary for ribosome assembly and cell growth"],"prefix":"10.1083","volume":"208","author":[{"given":"Homa","family":"Ghalei","sequence":"first","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"}]},{"given":"Franz X.","family":"Schaub","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"},{"name":"Department of Tumor Biology, Moffitt Cancer and Research Institute, Tampa, FL 33612 3"}]},{"given":"Joanne R.","family":"Doherty","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"}]},{"given":"Yoshihiko","family":"Noguchi","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"}]},{"given":"William R.","family":"Roush","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"}]},{"given":"John L.","family":"Cleveland","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology 1 and 2"},{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458 1 and 2"},{"name":"Department of Tumor Biology, Moffitt Cancer and Research Institute, Tampa, FL 33612 3"}]},{"given":"M. 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