Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and beta 4 integrin, hemidesmosomal components of basal keratinocytes.

Bullous pemphigoid antigen 2 (BPAG2/BP180, also known as type XVII collagen) and alpha 6 beta 4 integrin are both transmembrane proteins and hemidesmosomal components of basal keratinocytes. In this study, using yeast two-hybrid system, we demonstrate direct protein-protein interaction between the intracellular domains of BP180 and the beta 4 integrin ...
subunit. Detailed analysis revealed that a bait construct spanning amino acids 13-89 of BP180 contained sufficient information for the protein protein interaction, but further deletion of 13 amino-terminal amino acids, which eliminates a predicted beta-sheet, abolished the interaction. The intracellular domain of the beta 4 integrin subunit contains two pairs of fibronectin type III (FNIII) repeats separated by a connecting segment. Series of expression constructs, sequentially deleting each domain, revealed that the connecting segment, the second pair of FNIII repeats and the tail region of the beta 4 integrin subunit were necessary for the interaction with BP180 in yeast two-hybrid system.
Mesh Terms:
Alternative Splicing, Amino Acid Sequence, Antigens, Surface, Autoantigens, Carrier Proteins, Cell Membrane, Cells, Cultured, Collagen, Cytoskeletal Proteins, DNA-Binding Proteins, Fibronectins, Humans, Integrin alpha6beta4, Integrins, Keratinocytes, Molecular Sequence Data, Nerve Tissue Proteins, Non-Fibrillar Collagens, Polymerase Chain Reaction, Protein Structure, Secondary, RNA-Directed DNA Polymerase, Recombinant Fusion Proteins, Repetitive Sequences, Nucleic Acid, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Biochem. Biophys. Res. Commun.
Date: Feb. 24, 1998
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