Extracellular domains binding mechanism with

Fig. 5 Possible motions of the type II receptors during interaction with the TGF-fS ligand. Binding of the ligand to the T RII receptor homodimer induces rotation and swinging of the extracellular domains, which are translated through the transmembrane parts into rearrangements of intracellular domains by means of a flexible rotation mechanism, finally causing dissolution of the dimer and spatial separation of the receptor monomers...

On such modified surfaces, some of the attached proteins are recognized by cytoskeletally associated receptors in the cell membrane. So, in the end, the extracellular substrate is mechanically connected with the intracellular cytoskele-ton, which may secrete its own adhesion proteins. Integrins, as an important class of cell receptors [63], bind to small domains on their adhesion proteins, e.g., the oligopeptide sequence arginine-glycine-aspartic acid (RGD) that is common in fibronectin [64],... 

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