Phosducin and monomeric β-actin have common epitope recognized by anti-phosducin antibodies.

Phosducin family proteins are regulators of cytoplasmic processes. The main function ascribed to phosducin is the binding and sequestration of the β subunit of heterotrimeric G proteins. Phosducin-like protein 1, longer than phosducin by 37 amino-acids, is involved in chaperoning of newly synthesized proteins. β-Actin, a component of the cytoskeleton, participates in cell movement. There is no apparent evolutionary relationship between phosducin and β-actin nor structure similarity. Nevertheless we obtained the polyclonal antibodies named ap33, originally directed against a phosducin-derived peptide (SQSLEEDFEGQATHTGPK), that also recognized β-actin. The epitope on the β-actin molecule was characterized. It is a conformational epitope grouping some of the L-D-F-E-Q-A-T-K amino-acids found in the peptide originally used to obtain the antibodies. The main part of the epitope is localized on the actin-actin interface of polymerized actin, so it is accessible only on monomeric actin. The existence of a common epitope on the molecules of phosducin and β-actin may reflect a topological similarity of a small region of their surfaces.

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