Antibodies to synthetic peptides from the tubulin regulatory domain interact with tubulin and microtubules.

Vera JC, Rivas CI, Maccioni RB.

Abstract

A fundamental question in microtubule research is how the interactions of tubulin subunits with microtubule-associated proteins (MAPs) are controlled. The answer should provide insight into the regulation of the cellular processes in which microtubules are implicated. Previous work demonstrated the interaction of MAPs with a 4-kDa C-terminal domain of tubulin alpha and beta subunits. Synthetic peptides from the variable region of the 4-kDa C-terminal moiety of tubulin subunits, alpha-(430-441) and beta-(422-434), bind to MAP-2 and to the MAP tau, and a preferential interaction of the beta peptide is observed. To define the regulatory significance of the substructure of the C-terminal tubulin domain, we produced rabbit antisera against these MAP-interacting peptides. We found that these antisera contained not only antibodies to the original synthetic peptides but also antibodies to MAPs. Here, we report that these antibodies, which react with MAP-1, MAP-2, and tau, appear to be a population of anti-idiotypic antibodies directed to the anti-peptide antibodies. They can inhibit MAP-induced tubulin assembly into microtubules in vitro, and the addition of MAPs overcomes the inhibition. The recognition by these anti-idiotypic antibodies of the tubulin-binding domain on MAPs provides unequivocal evidence that the tubulin region defined by the synthetic peptides is directly involved in the interaction with MAPs.

Más información

Título de la Revista: Proc Natl Acad Sci U S A
Volumen: 85
Número: 18
Fecha de publicación: 1988
Página de inicio: 6763
Página final: 6767
Idioma: English
DOI:

PMID: 2901104 [PubMed - indexed for MEDLINE] PMCID: PMC282058

Notas: ISI