COMMON AND DISTINCT TUBULIN BINDING-SITES FOR MICROTUBULE-ASSOCIATED PROTEINS

被引：220

作者：

LITTAUER, UZ ^{[1
]}

GIVEON, D ^{[1
]}

THIERAUF, M ^{[1
]}

GINZBURG, I ^{[1
]}

PONSTINGL, H ^{[1
]}

机构：

[1] GERMAN CANC RES CTR, INST CELL & TUMOR BIOL, PROJECT GRP MOLEC BIOL MITOSIS, D-6900 HEIDELBERG, FED REP GER

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1986年 / 83卷 / 19期

关键词：

D O I：

10.1073/pnas.83.19.7162

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 .tau. factors to 60 peptides derived from porcine .alpha.- and .beta.-tubulin. MAP2 and .tau. factors specifically interacted with two peptides derived from the carboxyl-terminal region of .beta.-tubulin, which are located between positions 392-445 and 416-445. In addition, there is a distinct .tau.-binding site at the amino-terminal region of .alpha.-tubulin. .tau. factors but not MAP2 displayed strong interaction with a peptide derived from the amino-terminal domain of .alpha.-tubulin between positions 1 and 75. To narrow down the location of the .beta.-tubulin binding site that is common to MAP2 and .tau. 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 .beta.-tubulin are crucial for the interaction of MAP2 and .tau. factors.

引用

页码：7162 / 7166

页数：5

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