{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T07:27:58Z","timestamp":1791271678287,"version":"4.1.0"},"reference-count":49,"publisher":"The Company of Biologists","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2003,1,15]]},"abstract":"<jats:p>Hemidesmosomes (HDs) are multi-protein complexes that promote stable adhesion of epithelial cells to the underlying extracellular matrix. We assessed the interactions between different hemidesmosomal components with each other, mapped the binding sites and studied the importance of these interactions for HD assembly in yeast two-hybrid and cell-transfection assays. The results show that: (1) bullous pemphigoid antigen (BP) 180 binds not only to BP230, but also to plectin. The interactions between these proteins are facilitated by the Y subdomain in the N-terminal plakin domain of BP230 and plectin, and residues 145-230 of the cytoplasmic domain of BP180; (2) different, but overlapping, sequences on BP180 mediate binding to \u03b24, which, in turn associates with BP180 via its third fibronectin type III repeat; (3) sequences in the N-terminal extremity of BP230 mediate its binding to \u03b24, which requires the C-terminal end of the connecting segment up to the fourth FNIII repeat of the \u03b24 subunit. (4) Finally, cell-transfection studies showed that the localization of BP230 into hemidesmosome-like structures depends on its Z-Y subdomains as well as on the availability of BP180. By having further uncovered interactions between various hemidesmosomal components, mapped the involved binding sites and dissected a hierarchy of interactions relevant for their topogenic fate, our findings give novel insights into the molecular organization of hemidesmosomes.<\/jats:p>","DOI":"10.1242\/jcs.00241","type":"journal-article","created":{"date-parts":[[2002,12,13]],"date-time":"2002-12-13T18:22:55Z","timestamp":1039803775000},"page":"387-399","source":"Crossref","is-referenced-by-count":199,"title":["Analysis of the interactions between BP180, BP230, plectin and the integrin \u03b16\u03b24 important for hemidesmosome assembly"],"prefix":"10.1242","volume":"116","author":[{"given":"Jan","family":"Koster","sequence":"first","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Geerts","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"},{"name":"Present address: Department of Human Genetics, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ, Amsterdam"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bertrand","family":"Favre","sequence":"additional","affiliation":[{"name":"University Hospital Geneva, Department of Dermatology, CH-1211 Geneva, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luca","family":"Borradori","sequence":"additional","affiliation":[{"name":"University Hospital Geneva, Department of Dermatology, CH-1211 Geneva, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnoud","family":"Sonnenberg","sequence":"additional","affiliation":[{"name":"The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042517464253300_REF1","doi-asserted-by":"crossref","unstructured":"Aho, S. and Uitto, J. (1998). Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and \u03b24 integrin, hemidesmosomal components of basal keratinocytes. Biochem. Biophys. Res. Commun.243, 694-699.","DOI":"10.1006\/bbrc.1998.8162"},{"key":"2021042517464253300_REF2","doi-asserted-by":"crossref","unstructured":"Andra\u0308, K., Lassmann, H., Bittner, R., Shorny, S., Fa\u0308ssler, R., Propst, F. and Wiche, G. (1997). Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev.11, 3143-3156.","DOI":"10.1101\/gad.11.23.3143"},{"key":"2021042517464253300_REF3","doi-asserted-by":"crossref","unstructured":"Borradori, L. and Sonnenberg, A. (1999). Structure and function of hemidesmosomes: more than simple adhesion complexes. J. Invest. 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