Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca2+-dependent, low-affinity trans-interaction

Jens Waschke, Carlos Menendez-Castro, Paola Bruggeman, Rainer Koob, Masayuki Amagai, Hermann J. Gruber, Detlev Drenckhahn, Werner Baumgartner

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)


Desmoglein 1 is a desmosomal member of the cadherin family expressed in stratified epithelia. Desmoglein 1 is the target adhesion molecule of severe blistering skin diseases such as pemphigus or bullous impetigo. However, despite this enormous pathological relevance, the molecular binding properties of desmoglein 1 are largely unknown. Using atomic force microscopic imaging, we found that desmoglein 1 molecules displayed Ca2+-dependent conformational changes of the extracellular domains. By single-molecule force-distance cycles, we provide evidence that desmoglein 1 undergoes Ca 2+-dependent (K d = 0.8 mm Ca2+) homophilic trans-interaction, which is highly relevant for the contribution of desmoglein 1 homophilic binding to keratinocyte cohesion in distinct epidermal layers. Moreover, while the single-unit unbinding force is comparable to other cadherins (∼40 pN at retrace velocity of 300 nm/s), apparent differences with respect to multivalency of interaction and lifetime of single bonds (0.17 s) were observed. Thus, besides the biophysical characterization of desmoglein 1, a main outcome of the study is that desmoglein 1 differs from other members of the cadherin family in terms of some molecular binding properties.

Original languageEnglish
Pages (from-to)83-92
Number of pages10
JournalJournal of Membrane Biology
Issue number2-3
Publication statusPublished - 2007 Apr


  • Atomic force microscopy
  • Cadherin
  • Cell adhesion
  • Desmosome
  • Pemphigus

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology


Dive into the research topics of 'Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca<sup>2+</sup>-dependent, low-affinity trans-interaction'. Together they form a unique fingerprint.

Cite this