Allosteric cross talk between cadherin extracellular domains

Quanming Shi, Venkat Maruthamuthu, Fang Li, Deborah E Leckband

Research output: Contribution to journalArticle

Abstract

Atomic force microscopy and surface force apparatus measurements determined the functional impact of the cadherin point mutation W2A and domain deletion mutations on C-cadherin binding signatures. Direct comparison of results obtained using both experimental approaches demonstrates that C-cadherin ectodomains form multiple independent bonds that require different structural regions. The results presented reveal significant interdomain cross talk. They further demonstrate that the mutation W2A not only abolishes adhesion between N-terminal domains, but allosterically modulates other binding states that require functional domains distal to the N-terminal binding site. Such allosteric effects may play a prominent role in modulating adhesion by Type I classic cadherins, cadherin oligomerization at junctional contacts, and propagation of binding information to the cytoplasmic region.

Original languageEnglish (US)
Pages (from-to)95-104
Number of pages10
JournalBiophysical journal
Volume99
Issue number1
DOIs
StatePublished - Jul 7 2010

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Cadherins
Atomic Force Microscopy
Sequence Deletion
Point Mutation
Binding Sites
Mutation

ASJC Scopus subject areas

  • Biophysics

Cite this

Allosteric cross talk between cadherin extracellular domains. / Shi, Quanming; Maruthamuthu, Venkat; Li, Fang; Leckband, Deborah E.

In: Biophysical journal, Vol. 99, No. 1, 07.07.2010, p. 95-104.

Research output: Contribution to journalArticle

Shi, Quanming ; Maruthamuthu, Venkat ; Li, Fang ; Leckband, Deborah E. / Allosteric cross talk between cadherin extracellular domains. In: Biophysical journal. 2010 ; Vol. 99, No. 1. pp. 95-104.
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