{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:20:22Z","timestamp":1779344422739,"version":"3.51.4"},"reference-count":0,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[1997,12,1]],"date-time":"1997-12-01T00:00:00Z","timestamp":880934400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[1997,12]]},"abstract":"<jats:p>\n                    The modification of cytosolic proteins with polyubiquitin chains targets them for recognition and degradation by the multisubunit proteolytic particle, the 26S proteasome. Membrane proteins are also substrates for ubiquitination. Integral membrane proteins of the endoplasmic reticulum are ubiquitinated and destroyed by the proteasome (reviewed in refs 1, 2). However, it has been shown recently that the ubiquitination of\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    plasma membrane proteins signals their degradation by the proteolytic system in the lysosome\u2010like vacuole. Ubiquitination of several different classes of cell surface proteins serves as a signal for their entry into the endocytic pathway; this leads to their transport to the vacuole, where they are permanently inactivated by degradation. In yeast, ubiquitin has been implicated as an internalization signal for most, if not all, endogenous plasma membrane proteins that are known to be endocytosed. Ubiquitin\u2010dependent internalization has been best characterized for two proteins: the mating pheromone \u03b1\u2010factor receptor and the uracil permease. Some mammalian cell surface receptors are also ubiquitinated at the plasma membrane. Ubiquitination machinery is required for ligand\u2010induced endocytosis of the growth hormone receptor, suggesting that ubiquitin\u2010dependent endocytosis and sorting is also an important regulatory process in mammalian cells. Mammalian receptors may also be down\u2010regulated through the degradation of their cytosolic domains by a proteasome\u2010dependent pathway.\u2014Hicke, L. Ubiquitin\u2010dependent internalization and down\u2010regulation of plasma membrane proteins.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    11, 1215\u20131226 (1997)\n                  <\/jats:p>","DOI":"10.1096\/fasebj.11.14.9409540","type":"journal-article","created":{"date-parts":[[2018,1,18]],"date-time":"2018-01-18T06:05:22Z","timestamp":1516255522000},"page":"1215-1226","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":227,"title":["Ubiquitin\u2010dependent internalization and down\u2010regulation of plasma membrane proteins"],"prefix":"10.1096","volume":"11","author":[{"given":"Linda","family":"Hicke","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Molecular Biology, and Cell Biology Northwestern University Evanston Illinois 60208\u20133500 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[1997,12]]},"container-title":["The FASEB Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1096\/fasebj.11.14.9409540","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/faseb.onlinelibrary.wiley.com\/doi\/pdf\/10.1096\/fasebj.11.14.9409540","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T16:35:15Z","timestamp":1761669315000},"score":1,"resource":{"primary":{"URL":"https:\/\/faseb.onlinelibrary.wiley.com\/doi\/10.1096\/fasebj.11.14.9409540"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,12]]},"references-count":0,"journal-issue":{"issue":"14","published-print":{"date-parts":[[1997,12]]}},"alternative-id":["10.1096\/fasebj.11.14.9409540"],"URL":"https:\/\/doi.org\/10.1096\/fasebj.11.14.9409540","archive":["Portico"],"relation":{},"ISSN":["0892-6638","1530-6860"],"issn-type":[{"value":"0892-6638","type":"print"},{"value":"1530-6860","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,12]]},"assertion":[{"value":"1997-12-01","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}