Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein.
While evidence is mounting that cells exploit protein unfolding for mechanochemical signal conversion (mechanotransduction), what mechanisms are in place to deal with the unwanted consequences of exposing hydrophobic residues upon force-induced protein unfolding? Here, we show that mechanical chaperones exist that can transiently bind to hydrophobic residues that are freshly exposed by mechanical force. The stretch-upregulated binding of albumin or casein to fibronectin fibers is reversible and does not inhibit fiber contraction once the tension is released.
Little
William C
WC
Department of Materials, ETH Zurich, CH-8093 Zurich, Switzerland.
Schwartlander
Ruth
R
Smith
Michael L
ML
Gourdon
Delphine
D
Vogel
Viola
V
D001665:Binding Sites; D002364:Caseins / Q000737:chemistry* / Q000648:ultrastructure*; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D018832:Molecular Chaperones / Q000737:chemistry / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D012709:Serum Albumin / Q000737:chemistry* / Q000648:ultrastructure*; D013314:Stress, Mechanical
D002364:Caseins; D016326:Extracellular Matrix Proteins; D018832:Molecular Chaperones; D012709:Serum Albumin