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Published 25 September 2006. doi:10.1083/jcb.200609029
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 7, 911-913
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For catch bonds, it all hinges on the interdomain region



Wendy Thomas

Department of Bioengineering, University of Washington, Seattle, WA 98195

Correspondence to Wendy Thomas: wendyt{at}u.washington.edu


Abstract

Tensile mechanical force was long assumed to increase the detachment rates of biological adhesive bonds (Bell, 1978). However, in the last few years, several receptor–ligand pairs were shown to form "catch bonds," whose lifetimes are enhanced by moderate amounts of force. These include the bacterial adhesive protein FimH binding to its ligand mannose (Thomas et al., 2002; Thomas et al., 2006), blood cell adhesion proteins P- and L-selectin binding to sialyl Lewis X (sLeX)–containing ligands (Marshall et al., 2003; Evans et al., 2004; Sarangapani et al., 2004), and the myosin–actin motor protein interaction (Guo and Guilford, 2006). The structural mechanism behind this counterintuitive force–enhanced catch bond behavior is of great interest.

Abbreviations used in this paper: PSGL, P-selectin glycoprotein ligand; sLeX, sialyl Lewis X; SPR, surface plasmon resonance.


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