{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,20]],"date-time":"2026-01-20T15:38:25Z","timestamp":1768923505312,"version":"3.49.0"},"reference-count":80,"publisher":"Rockefeller University Press","issue":"7","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1999,6,28]]},"abstract":"<jats:p>Caveolins are integral membrane proteins which are a major component of caveolae. In addition, caveolins have been proposed to cycle between intracellular compartments and the cell surface but the exact trafficking route and targeting information in the caveolin molecule have not been defined. We show that antibodies against the caveolin scaffolding domain or against the COOH terminus of caveolin-1 show a striking specificity for the Golgi pool of caveolin and do not recognize surface caveolin by immunofluorescence. To analyze the Golgi targeting of caveolin in more detail, caveolin mutants were expressed in fibroblasts. Specific mutants lacking the NH2 terminus were targeted to the cis Golgi but were not detectable in surface caveolae. Moreover, a 32\u2013amino acid segment of the putative COOH-terminal cytoplasmic domain of caveolin-3 was targeted specifically and exclusively to the Golgi complex and could target a soluble heterologous protein, green fluorescent protein, to this compartment. Palmitoylation-deficient COOH-terminal mutants showed negligible association with the Golgi complex. This study defines unique Golgi targeting information in the caveolin molecule and identifies the cis Golgi complex as an intermediate compartment on the caveolin cycling pathway.<\/jats:p>","DOI":"10.1083\/jcb.145.7.1443","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"1443-1459","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":111,"title":["Molecular Characterization of Caveolin Association with the Golgi Complex: Identification of a Cis-Golgi Targeting Domain in the Caveolin Molecule"],"prefix":"10.1083","volume":"145","author":[{"given":"Robert","family":"Luetterforst","sequence":"first","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Espen","family":"Stang","sequence":"additional","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natasha","family":"Zorzi","sequence":"additional","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amanda","family":"Carozzi","sequence":"additional","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Way","sequence":"additional","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert G.","family":"Parton","sequence":"additional","affiliation":[{"name":"*Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Queensland 4072, Australia; and \u2021European Molecular Biology Laboratory, 69012 Heidelberg, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1999,6,28]]},"reference":[{"key":"2023072900342970000_B1","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1146\/annurev.biochem.67.1.199","article-title":"The caveolae membrane system","volume":"67","author":"Anderson","year":"1998","journal-title":"Annu Rev Biochem"},{"key":"2023072900342970000_B2","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0955-0674(93)90135-D","article-title":"Plasmalemmal caveolae and GPI-anchored proteins","volume":"5","author":"Anderson","year":"1993","journal-title":"Curr Opin Cell Biol"},{"key":"2023072900342970000_B3","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.1091\/mbc.7.11.1825","article-title":"Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae","volume":"7","author":"Anderson","year":"1996","journal-title":"Mol Biol Cell"},{"key":"2023072900342970000_B4","doi-asserted-by":"crossref","first-page":"10693","DOI":"10.1073\/pnas.94.20.10693","article-title":"Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol","volume":"94","author":"Bist","year":"1997","journal-title":"Proc Natl Acad Sci USA"},{"key":"2023072900342970000_B5","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1016\/S0021-9258(19)69848-0","article-title":"Phase separation of integral membrane proteins in Triton X-114 solution","volume":"256","author":"Bordier","year":"1981","journal-title":"J Biol Chem"},{"key":"2023072900342970000_B6","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1002\/j.1460-2075.1994.tb06514.x","article-title":"Retrieval of trans Golgi network proteins from the cell surface requires endosomal acidification","volume":"13","author":"Chapman","year":"1994","journal-title":"EMBO (Eur Mol Biol Organ) J"},{"key":"2023072900342970000_B7","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0092-8674(90)90369-P","article-title":"Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments","volume":"62","author":"Chavrier","year":"1990","journal-title":"Cell"},{"key":"2023072900342970000_B8","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1083\/jcb.131.6.1421","article-title":"Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps","volume":"131","author":"Conrad","year":"1995","journal-title":"J Cell Biol"},{"key":"2023072900342970000_B9","doi-asserted-by":"crossref","first-page":"6838","DOI":"10.1074\/jbc.270.12.6838","article-title":"Caveolin is palmitoylated on multiple cysteine residues. 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