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Title

Architecture of hemidesmosomes

AuthorsManso, José A. ; Carabias, Arturo ; Gómez-Hernández, María ; García-Rubio, Inés; Sonnenberg, Arnoud; Pereda, José M. de
Issue Date2016
PublisherSociedad Española de Bioquímica y Biología Molecular
CitationXXXIX Congreso SEBBM (2016)
AbstractHemidesmosomes (HDs) are junctional complexes that mediate stable attachment of epithelial cells to the basal lamina, linking the extracellular matrix to the cytokeratins. In stratified epithelia HDs are composed of integrin α6β4, the bullous pemphigoid antigen 2 (BPAG2), tetraspanin CD151, and two proteins of the plakin family: plectin and BPAG1e. The integrin α6β4 is a receptor for laminins and a central hub of the HD protein network. The intracellular interactions of α6β4 are mediated by the cytodomain of the β4 subunit. Plectin and BPAG1e bind to β4 via their N-terminal regions and to cytokeratins via their C-terminal domains. Defects in HD-proteins cause several types of the blistering disease epidermolysis bullosa. Our long-term goal is to understand the organization and regulation of HDs. Previously, we had characterized the structure of the plectin-integrin β4 complex. Now we have elucidated the structural basis of the BPAG1e-β4 interaction. Binding occurs between an N-terminal segment of BPAG1e and the third and fourth fibronectin type III domains (FnIII-3,4) of β4. Ser residues in BPAG1e are involved in the binding interface, suggesting that the interaction may be regulated by phosphorylation. Complementing the analysis of hetero-interactions, we have elucidated the structure of dimeric plakins. Similarly to most plakins, plectin has an N-terminal “plakin domain” formed by spectrin repeats that adopt an elongated structure, which is followed by a central coiled-coil rod domain that mediates dimerization. The plakin domains are arranged in parallel in the homo-dimer. Thus, the distance between the β4 binding-sites is restricted, suggesting that the avidity-mediated stabilization of the interaction might be linked to the clustering of α6β4 in the membrane.
DescriptionResumen del póster presentado al XXXIX Congreso de la Sociedad Española de Bioquímica y Biología Molecular, celebrado en Salamanca del 5 al 8 de septiembre de 2016.
URIhttp://hdl.handle.net/10261/169469
Appears in Collections:(IBMCC) Comunicaciones congresos
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