{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T09:31:45Z","timestamp":1791279105916,"version":"4.1.0"},"reference-count":79,"publisher":"Rockefeller University Press","issue":"4","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2000,5,15]]},"abstract":"<jats:p>CD151 is a cell surface protein that belongs to the tetraspan superfamily. It associates with other tetraspan molecules and certain integrins to form large complexes at the cell surface. CD151 is expressed by a variety of epithelia and mesenchymal cells. We demonstrate here that in human skin CD151 is codistributed with \u03b13\u03b21 and \u03b16\u03b24 at the basolateral surface of basal keratinocytes. Immunoelectron microscopy showed that CD151 is concentrated in hemidesmosomes. By immunoprecipitation from transfected K562 cells, we established that CD151 associates with \u03b13\u03b21 and \u03b16\u03b24. In \u03b24-deficient pyloric atresia associated with junctional epidermolysis bullosa (PA-JEB) keratinocytes, CD151 and \u03b13\u03b21 are clustered together at the basal cell surface in association with patches of laminin-5. Focal adhesions are present at the periphery of these clusters, connected with actin filaments, and they contain both CD151 and \u03b13\u03b21. Transient transfection studies of PA-JEB cells with \u03b24 revealed that the integrin \u03b16\u03b24 becomes incorporated into the \u03b13\u03b21-CD151 clusters where it induces the formation of hemidesmosomes. As a result, the amount of \u03b13\u03b21 in the clusters diminishes and the protein becomes restricted to the peripheral focal adhesions. Furthermore, CD151 becomes predominantly associated with \u03b16\u03b24 in hemidesmosomes, whereas its codistribution with \u03b13\u03b21 in focal adhesions becomes partial. The localization of \u03b16\u03b24 in the pre-hemidesmosomal clusters is accompanied by a strong upregulation of CD151, which is at least partly due to increased cell surface expression. Using \u03b24 chimeras containing the extracellular and transmembrane domain of the IL-2 receptor and the cytoplasmic domain of \u03b24, we found that for recruitment of CD151 into hemidesmosomes, the \u03b24 subunit must be associated with \u03b16, confirming that integrins associate with tetraspans via their \u03b1 subunits. CD151 is the only tetraspan identified in hemidesmosomal structures. Others, such as CD9 and CD81, remain diffusely distributed at the cell surface.<\/jats:p>\n               <jats:p>In conclusion, we show that CD151 is a major component of (pre)-hemidesmosomal structures and that its recruitment into hemidesmosomes is regulated by the integrin \u03b16\u03b24. We suggest that CD151 plays a role in the formation and stability of hemidesmosomes by providing a framework for the spatial organization of the different hemidesmosomal components.<\/jats:p>","DOI":"10.1083\/jcb.149.4.969","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"969-982","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":209,"title":["The Tetraspan Molecule Cd151, a Novel Constituent of Hemidesmosomes, Associates with the Integrin \u03b16\u03b24 and May Regulate the Spatial Organization of Hemidesmosomes"],"prefix":"10.1083","volume":"149","author":[{"given":"Lotus M.Th.","family":"Sterk","sequence":"first","affiliation":[{"name":"aDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cecile A.W.","family":"Geuijen","sequence":"additional","affiliation":[{"name":"aDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauran C.J.M.","family":"Oomen","sequence":"additional","affiliation":[{"name":"bDivision of Biophysics, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jero","family":"Calafat","sequence":"additional","affiliation":[{"name":"aDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"Janssen","sequence":"additional","affiliation":[{"name":"aDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnoud","family":"Sonnenberg","sequence":"additional","affiliation":[{"name":"aDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2000,5,15]]},"reference":[{"key":"2023072209431996000_N0x2d81850N0x3571fc0","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/BF00188787","article-title":"Association of four antigens of the tetraspans family (CD37, CD53, TAPA- 1, and R2\/C33) with MHC class II glycoproteins","volume":"39","author":"Angelisov\u00e1","year":"1994","journal-title":"Immunogenetics."},{"key":"2023072209431996000_Ashmanetal1997"},{"key":"2023072209431996000_AumailleyandRouselle1999","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0945-053X(98)00004-3","article-title":"Laminins of the dermo-epidermal junction","volume":"18","author":"Aumailley","year":"1999","journal-title":"Matrix Biol."},{"key":"2023072209431996000_Berditchevskietal1995","doi-asserted-by":"crossref","first-page":"17784","DOI":"10.1074\/jbc.270.30.17784","article-title":"Specific association of CD63 with the VLA-3 and VLA-6 integrins","volume":"270","author":"Berditchevski","year":"1995","journal-title":"J. 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