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Molecular architecture and function of the hemidesmosome

Research output: Contribution to journalArticlepeer-review

Gernot Walko, Maria J. Castañón, Gerhard Wiche

Original languageEnglish
Pages (from-to)363-378
JournalCell and Tissue Research
Volume360
Issue number2
Early online date9 Dec 2014
DOIs
Accepted/In press3 Nov 2014
E-pub ahead of print9 Dec 2014
PublishedMay 2016

Documents

  • Molecular architecture and_WALKO_Accepted 3Nov2014_GOLD VoR

    Molecular_architecture_and_WALKO_Published_May2015_GOLD_VoR.pdf, 2.46 MB, application/pdf

    Uploaded date:23 Aug 2016

    Version:Final published version

    Licence:CC BY

    This article is distributed under the terms of the Creative
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King's Authors

Abstract

Hemidesmosomes are multiprotein complexes that facilitate the stable adhesion of basal epithelial cells to the underlying basement membrane. The mechanical stability of hemidesmosomes relies on multiple interactions of a few protein components that form a membrane-embedded tightly- ordered complex. The core of this complex is provided by integrin α6β4 and P1a, an isoform of the cytoskeletal linker protein plectin that is specifically associated with hemidesmosomes. Integrin α6β4 binds to the extracellular matrix protein laminin-332, whereas P1a forms a bridge to the cytoplasmic keratin intermediate filament network. Other important components are BPAG1e, the epithelial isoform of bullous pemphigoid antigen 1, BPAG2, a collagen-type transmembrane protein and CD151. Inherited or acquired diseases in which essential components of the hemidesmosome are missing or structurally altered result in tissue fragility and blistering. Modulation of hemidesmosome function is of crucial importance for a variety of biological processes, such as terminal differentiation of basal keratinocytes and keratinocyte migration during wound healing and carcinoma invasion. Here, we review the molecular characteristics of the proteins that make up the hemidesmosome core structure and summarize the current knowledge about how their assembly and turnover are regulated by transcriptional and posttranslational mechanisms.

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