The Microtubule-Associated Protein Tau Cross-Links to Two Distinct Sites on Each and ![]()
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- 作者：Miu-Fun Chau ; Monte J. Radeke ; Concepció ; n de Iné ; s ; Isabel Barasoain ; Lori A. Kohlstaedt ; and Stuart C. Feinstein
- 刊名：Biochemistry
- 出版年：1998
- 出版时间：December 22, 1998
- 年：1998
- 卷：37
- 期：51
- 页码：17692 - 17703
- 全文大小：203K
- 年卷期：v.37,no.51(December 22, 1998)
- ISSN：1520-4995
文摘
The interaction between tubulin subunits and microtubule-associated proteins (MAPs) suchas tau is fundamental for microtubule structure and function. Previous work has suggested that the"microtubule binding domain" of tau (composed of three or four imperfect 18-amino acid repeats, separatedby 13- or 14-amino acid inter-repeat regions) can bind to the C-terminal ends of both 
chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulinmonomers. Here, using covalent cross-linking strategies, we demonstrate that there are two distinct taucross-linking sites (designated as "C-terminal" and "internal") on each chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin monomer. TheC-terminal tau cross-linking site is located within the 12 C-terminal amino acids of both chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin,while the internal tau cross-linking site is located within the C-terminal one-third of chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin butnot within the last 12 amino acids. In addition, we show that tau cross-links to the C-terminal site via itsrepeat 1 and/or the R1-R2 inter-repeat. The cross-linking of tau to the internal site is mediated by somesubset of its other repeat units. Integrating these and earlier data with the 3.7 Å resolution model of thechars/alpha.gif" BORDER=0>chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin dimer recently presented by E. Nogales et al. [(1998), Nature 391, 199-203], we propose anew model for the tau-microtubule interaction.
chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulinmonomers. Here, using covalent cross-linking strategies, we demonstrate that there are two distinct taucross-linking sites (designated as "C-terminal" and "internal") on each chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin monomer. TheC-terminal tau cross-linking site is located within the 12 C-terminal amino acids of both chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin,while the internal tau cross-linking site is located within the C-terminal one-third of chars/alpha.gif" BORDER=0> and chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin butnot within the last 12 amino acids. In addition, we show that tau cross-links to the C-terminal site via itsrepeat 1 and/or the R1-R2 inter-repeat. The cross-linking of tau to the internal site is mediated by somesubset of its other repeat units. Integrating these and earlier data with the 3.7 Å resolution model of thechars/alpha.gif" BORDER=0>chars/beta2.gif" BORDER=0 ALIGN="middle"> tubulin dimer recently presented by E. Nogales et al. [(1998), Nature 391, 199-203], we propose anew model for the tau-microtubule interaction.