Nanomechanics of adhesion proteins

Current Opinion in Structural Biology

Volumn 14, Issue 5, 2004, Pages 524-530

  Leckband, Deborah ^a  

^a VA Chicago Hlth Care Syst W S   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; FIBRONECTIN; NERVE CELL ADHESION MOLECULE; NITRILOTRIACETIC ACID; P SELECTIN GLYCOPROTEIN LIGAND 1;

ACCURACY; ANALYTIC METHOD; ANTIGEN PRESENTING CELL; ATOMIC FORCE MICROSCOPY; CELL ADHESION; CHEMICAL BOND; CHEMICAL STRUCTURE; INTERFEROMETRY; MAJOR HISTOCOMPATIBILITY COMPLEX; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; REVIEW; SENSITIVITY ANALYSIS; SEPARATION TECHNIQUE; STRUCTURE ANALYSIS;

CELL ADHESION MOLECULES; MICROSCOPY, ATOMIC FORCE; NANOTECHNOLOGY; PROTEIN FOLDING;

EID: 4744348842     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.09.002     Document Type: Review

References (30)

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4. •,27], the proteins are pulled from the N and C termini. The force vector, or the direction of the gradient in the applied mechanical potential, biases the unfolding trajectory; the activation barrier along that trajectory determines the unfolding rate and hence the domain stability. However, protein folding or unfolding in solution may proceed by several pathways, many of which could have lower activation barriers than those probed in the mechanical measurement. These authors tested this idea by changing the ubiquitin attachment points in the pulling experiment. They showed that the unfolding force was lower relative to that measured when ubiquitin was pulled along the N to C axis. They thus demonstrated that the mechanical stability (or unfolding rate) of a protein also depends on how the force is applied to the molecule.
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24. C.P. Johnson, I. Fujimoto, C. Perrin-Tricaud, U. Rutishauser, and D. Leckband Mechanism of homophilic NCAM adhesion: use of multiple domains and flexibility Proc Natl Acad Sci USA 101 2004 6963 6968 Surface force measurements discriminated between three different models proposed for the mechanism of homophilic NCAM adhesion. Because the NCAM complexes in each of the three models spanned different membrane gaps, the SFA measurements readily tested each of the proposed mechanisms. In this study, the distance resolution of the SFA resulted in the measurement of two spatially distinct adhesive bonds between NCAM ectodomains. This confirmed that NCAM has multiple adhesive domains. Additional force and equilibrium binding measurements with Ig domain deletion mutants then identified the NCAM domains that generate the two independent bound states revealed by the force measurements.
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30. ••], whereby the force is held constant and the lifetime is measured at each constant force. In this case, they measured the bond strength as a function of the logarithm of the constant loading rate (dF/dt). They found that the strength increases logarithmically with dF/dt at >300 pN/s. This indicates that bond rupture follows a single kinetic path. However, at dF/dt <300 pN/s, the bond strength falls abruptly, suggesting that rupture occurs by a different unbinding pathway. To determine what governs this mechanical switching, the authors altered the force history of the bonds, by first rapidly 'jumping' the force by 20-30 pN. This jump was then followed by a steady force 'ramp' dF/dt. This initial 20-30 pN tug triggered bond strengthening, even at loading rates <300 pN/s. This is another demonstration that the mechanochemical response to force depends on the force history. It also illustrates that this protein pair acts as a mechanical switch, which enables these proteins to respond in different ways to subtle changes in the mechanical stimuli encountered in vivo.