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Common and Distinct Tubulin Binding Sites for Microtubule-Associated Proteins

Uriel Z. Littauer, David Giveon, Marion Thierauf, Irith Ginzburg and Herwig Ponstingl
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 19 (Oct. 1, 1986), pp. 7162-7166
Stable URL: http://www.jstor.org/stable/28430
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Common and Distinct Tubulin Binding Sites for Microtubule-Associated Proteins
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Abstract

A specific binding assay was developed that monitors the interaction of 125I-labeled microtubule-associated proteins (MAPs) with tubulin or its fragments bound to nitrocellulose membrane. To identify the tubulin-binding domains for MAPs we have examined the binding of rat brain 125I-labeled MAP2 or 125I-labeled τ factors to 60 peptides derived from porcine α - and β -tubulin. MAP2 and τ factors specifically interacted with two peptides derived from the carboxyl-terminal region of β -tubulin, which are located between positions 392-445 and 416-445. In addition, there is a distinct τ -binding site at the amino-terminal region of α -tubulin. τ factors but not MAP2 displayed strong interaction with a peptide derived from the amino-terminal domain of α -tubulin between positions 1 and 75. To narrow down the location of the β -tubulin binding site that is common to MAP2 and τ factors, we have synthesized five peptides that are homologous to the corresponding sequence from the porcine or rat carboxyl-terminal region. Binding studies with the synthetic peptides suggest that amino acid residues 434-440 of β -tubulin are crucial for the interaction of MAP2 and τ factors.

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