{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T13:57:57Z","timestamp":1791813477700,"version":"4.3.4"},"reference-count":85,"publisher":"Rockefeller University Press","issue":"1","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,7,13]]},"abstract":"<jats:p>Hemidesmosomes (HDs) are stable anchoring structures that mediate the link between the intermediate filament cytoskeleton and the cell substratum. We investigated the contribution of various segments of the \u03b24 integrin cytoplasmic domain in the formation of HDs in transient transfection studies using immortalized keratinocytes derived from an epidermolysis bullosa patient deficient in \u03b24 expression. We found that the expression of wild-type \u03b24 restored the ability of the \u03b24-deficient cells to form HDs and that distinct domains in the NH2- and COOH-terminal regions of the \u03b24 cytoplasmic domain are required for the localization of HD1\/plectin and the bullous pemphigoid antigens 180 (BP180) and 230 (BP230) in these HDs. The tyrosine activation motif located in the connecting segment (CS) of the \u03b24 cytoplasmic domain was dispensable for HD formation, although it may be involved in the efficient localization of BP180. Using the yeast two-hybrid system, we could demonstrate a direct interaction between \u03b24 and BP180 which involves sequences within the COOH-terminal part of the CS and the third fibronectin type III (FNIII) repeat. Immunoprecipitation studies using COS-7 cells transfected with cDNAs for \u03b16 and \u03b24 and a mutant BP180 which lacks the collagenous extracellular domain confirmed the interaction of \u03b24 with BP180. Nevertheless, \u03b24 mutants which contained the BP180-binding region, but lacked sequences required for the localization of HD1\/plectin, failed to localize BP180 in HDs. Additional yeast two- hybrid assays indicated that the 85 COOH-terminal residues of \u03b24 can interact with the first NH2-terminal pair of FNIII repeats and the CS, suggesting that the cytoplasmic domain of \u03b24 is folded back upon itself. Unfolding of the cytoplasmic domain may be part of a mechanism by which the interaction of \u03b24 with other hemidesmosomal components, e.g., BP180, is regulated.<\/jats:p>","DOI":"10.1083\/jcb.142.1.271","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:47:50Z","timestamp":1027702070000},"page":"271-284","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":161,"title":["Hemidesmosome Formation Is Initiated by the \u03b24 Integrin Subunit, Requires Complex Formation of \u03b24 and HD1\/Plectin, and Involves a Direct Interaction between \u03b24 and the Bullous Pemphigoid Antigen 180"],"prefix":"10.1083","volume":"142","author":[{"given":"Roel Q.J.","family":"Schaapveld","sequence":"first","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luca","family":"Borradori","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"},{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Geerts","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel R.","family":"van Leusden","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ingrid","family":"Kuikman","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirjam G.","family":"Nievers","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carien M.","family":"Niessen","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renske D.M.","family":"Steenbergen","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.F.","family":"Snijders","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnoud","family":"Sonnenberg","sequence":"additional","affiliation":[{"name":"*Division of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; \u2021Department of Dermatology, University of Geneva, CH-1211 Geneva, Switzerland; and \u00a7Department of Pathology, University Hospital Vrije Universiteit, 1081 HV Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1998,7,13]]},"reference":[{"key":"2023072211180211100_B1","doi-asserted-by":"crossref","first-page":"3143","DOI":"10.1101\/gad.11.23.3143","article-title":"Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture","volume":"11","author":"Andr\u00e4","year":"1997","journal-title":"Genes Dev"},{"key":"2023072211180211100_B2","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":"36","author":"Baker","year":"1997","journal-title":"Cell Motil Cytoskeleton"},{"key":"2023072211180211100_B3","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/S0955-0674(96)80106-2","article-title":"Hemidesmosomes: roles in adhesion, signaling and human diseases","volume":"8","author":"Borradori","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"2023072211180211100_B4","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1083\/jcb.136.6.1333","article-title":"The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the \u03b24 integrin subunit","volume":"136","author":"Borradori","year":"1997","journal-title":"J Cell Biol"},{"key":"2023072211180211100_B5","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1006\/excr.1997.3923","article-title":"Role of the bullous pemphigoid antigen 180 (BP180) in the assembly of hemidesmosomes and cell adhesion. 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