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  • Molecular basis of interactions between integrin and plectina

    images24The hemidesmosomes are multifunctional multiprotein complex of great importance to the integrity of epithelia. Exercise of mediators of cell adhesion and confer resistance to mechanical stress, linking the extracellular matrix with cytokeratin filaments in the cell. They consist of three components transmembrane: α6β4 integrin, BP180-type collagen XVII and integrin-associated tetraspanina CD151. Integrin α6β4 is a receptor for laminin with high specificity for laminin-5, or basal membrane protein that binds to epidermal cytokeratin through plectina and BP230.

    The α6β4-plectina interaction is essential for the stability of the hemidesmosome and is believed to be the start of assembly of these adhesion complexes that anchor epithelial cells to the basement membrane. Most α6β44 interactions occur through the cytoplasmic half of the β4 subunit. The N-terminal region of plectina this subunit interacts with β4 in multiple zones. Two mutations in the gene for β4 (ITBG4) introduce R1225H and R1281W substitutions in one of the domains of β4 that prevent binding to plectina and lead to nonlethal forms of epidermolysis bullosa.

    These researchers led by de Pereda, University of Salamanca, have determined the structure of the complex primary α6β4-plectina. Combining mutagenesis and biophysical data have identified the critical elements of this interaction. They have also solved the crystal structure of the β4 subunit in the absence of plectina. This can confirm a conformational change b4 segment before joining plectina and suggests a form of allosteric control of integrin. These findings provide the molecular basis of certain diseases in which the targets are the assembly and stability of hemidesmosomes.

    Published on October 31, 2012 · Filed under: Bioscience; Tagged as: , , ,
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