{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:43:12Z","timestamp":1779342192280,"version":"3.51.4"},"reference-count":81,"publisher":"The Company of Biologists","issue":"12","license":[{"start":{"date-parts":[[1998,6,15]],"date-time":"1998-06-15T00:00:00Z","timestamp":897868800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1998,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Recently, we have shown that a region within the \u03b24 cytoplasmic domain, encompassing the second fibronectin type III (FNIII) repeat and the first 27 amino acids of the connecting segment, is critical for the localization of \u03b16\u03b24 in hemidesmosomes. In addition, this region was shown to regulate the distribution of HD1\/plectin in transfected cells. In order to investigate the function of the \u03b24 extracellular and cytoplasmic domains in the assembly and integrity of hemidesmosomes, we have constructed chimeric receptors consisting of the extracellular and transmembrane domains of the interleukin 2 receptor (IL2R), fused to different parts of the \u03b24 cytoplasmic domain. These chimeras are expressed as single subunits at the plasma membrane. The results show that the first and the second FNIII repeat, together with the first part of the connecting segment (in total a stretch of 241 amino acids spanning amino acids 1,115 to 1,356) are both essential and sufficient for the localization of \u03b24 in pre-existing hemidesmosomes. Moreover, expression of the IL2R\/\u03b24 chimeric constructs in COS-7 and CHO cells, which do not express \u03b16\u03b24 or the bullous pemphigoid (BP) antigens but do express HD1\/plectin, revealed that the stretch of 241 amino acids is sufficient for inducing the formation of type II hemidesmosomes. Expression of the IL2R\/\u03b24 chimeras in a keratinocyte cell line derived from a patient lacking \u03b24 expression, showed that amino acids 1,115 to 1,356 can also induce the formation of type I hemidesmosomes. We further demonstrate that type I and II hemidesmosomes can also be formed upon adhesion of \u03b16\u03b24-expressing cells to fibronectin. These findings establish that the \u03b24 extracellular domain is not essential for the induction of hemidesmosome assembly. Moreover, they demonstrate that binding of \u03b16\u03b24 to ligand, and heterodimerization of \u03b16 with \u03b24, are not required for hemidesmosome formation. This indicates that the assembly of hemidesmosomes can be regulated from within the cell.<\/jats:p>","DOI":"10.1242\/jcs.111.12.1659","type":"journal-article","created":{"date-parts":[[2021,4,24]],"date-time":"2021-04-24T05:30:17Z","timestamp":1619242217000},"page":"1659-1672","source":"Crossref","is-referenced-by-count":50,"title":["Ligand-independent role of the \u03b24 integrin subunit in the formation of hemidesmosomes"],"prefix":"10.1242","volume":"111","author":[{"given":"Mirjam G.","family":"Nievers","sequence":"first","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roel Q. J.","family":"Schaapveld","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lauran C. J. M.","family":"Oomen","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lionel","family":"Fontao","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dirk","family":"Geerts","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arnoud","family":"Sonnenberg","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1998,6,15]]},"reference":[{"key":"2024010623345282600_JOCES_111_12_1659C1","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1038\/ng0394-299","article-title":"Herlitz\u2019s junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the \u03b32 subunit of nicein\/kalinin (laminin-5)","volume":"6","author":"Aberdam","year":"1994","journal-title":"Nature Genet"},{"key":"2024010623345282600_JOCES_111_12_1659C2","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1002\/(SICI)1097-0169(1997)37:3<271::AID-CM9>3.0.CO;2-9","article-title":"Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: involvement of IFAP300\/HD1 and evidence that laminin-5\/cell interactions correlate with a dephosphorylation of \u03b16A integrin","volume":"37","author":"Baker","year":"1997","journal-title":"Cell Motil. 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