000131531 001__ 131531
000131531 005__ 20240212170624.0
000131531 0247_ $$2doi$$a10.1016/j.str.2019.03.016
000131531 0248_ $$2sideral$$a111672
000131531 037__ $$aART-2019-111672
000131531 041__ $$aeng
000131531 100__ $$aManso, José A.
000131531 245__ $$aIntegrin a6ß4 recognition of a linear motif of bullous pemphigoid antigen BP230 controls its recruitment to hemidesmosomes
000131531 260__ $$c2019
000131531 5060_ $$aAccess copy available to the general public$$fUnrestricted
000131531 5203_ $$aMechanical stability of epithelia requires firm attachment to the basement membrane via hemidesmosomes. Dysfunction of hemidesmosomal proteins causes severe skin-blistering diseases. Two plakins, plectin and BP230 (BPAG1e), link the integrin a6ß4 to intermediate filaments in epidermal hemidesmosomes. Here, we show that a linear sequence within the isoform-specific N-terminal region of BP230 binds to the third and fourth FnIII domains of ß4. The crystal structure of the complex and mutagenesis analysis revealed that BP230 binds between the two domains of ß4. BP230 induces closing of the two FnIII domains that are locked in place by an interdomain ionic clasp required for binding. Disruption of BP230-ß4 binding prevents recruitment of BP230 to hemidesmosomes in human keratinocytes, revealing a key role of this interaction for hemidesmosome assembly. Phosphomimetic substitutions in ß4 and BP230 destabilize the complex. Thus, our study provides insights into the architecture of hemidesmosomes and potential mechanisms of regulation.
000131531 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E35-20R$$9info:eu-repo/grantAgreement/EC/FP7/283570/EU/Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities/BIOSTRUCT-X$$9info:eu-repo/grantAgreement/ES/MEC/FPU14-06259$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2009-08389$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2015-69499-P$$9info:eu-repo/grantAgreement/ES/MINECO/CTQ2015-64486-R
000131531 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000131531 590__ $$a4.862$$b2019
000131531 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b64 / 296 = 0.216$$c2019$$dQ1$$eT1
000131531 591__ $$aBIOPHYSICS$$b9 / 71 = 0.127$$c2019$$dQ1$$eT1
000131531 591__ $$aCELL BIOLOGY$$b61 / 194 = 0.314$$c2019$$dQ2$$eT1
000131531 592__ $$a2.786$$b2019
000131531 593__ $$aStructural Biology$$c2019$$dQ1
000131531 593__ $$aMolecular Biology$$c2019$$dQ1
000131531 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/submittedVersion
000131531 700__ $$aGómez-Hernández, María
000131531 700__ $$aCarabias, Arturo
000131531 700__ $$aAlonso-García, Noelia
000131531 700__ $$0(orcid)0000-0002-1827-1250$$aGarcía-Rubio, Inés$$uUniversidad de Zaragoza
000131531 700__ $$aKreft, Maaike
000131531 700__ $$aSonnenberg, Arnoud
000131531 700__ $$aPereda, José M. de
000131531 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000131531 773__ $$g27, 6 (2019), 952-964.e6$$pStructure$$tStructure$$x0969-2126
000131531 8564_ $$s5470484$$uhttps://zaguan.unizar.es/record/131531/files/texto_completo.pdf$$yPreprint
000131531 8564_ $$s2876867$$uhttps://zaguan.unizar.es/record/131531/files/texto_completo.jpg?subformat=icon$$xicon$$yPreprint
000131531 909CO $$ooai:zaguan.unizar.es:131531$$particulos$$pdriver
000131531 951__ $$a2024-02-12-17:05:34
000131531 980__ $$aARTICLE