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Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex.

Abstract：

:Plus-end tracking proteins, such as EB1 and the dynein/dynactin complex, regulate microtubule dynamics. These proteins are thought to stabilize microtubules by forming a plus-end complex at microtubule growing ends with ill-defined mechanisms. Here we report the crystal structure of two plus-end complex components, the carboxy-terminal dimerization domain of EB1 and the microtubule binding (CAP-Gly) domain of the dynactin subunit p150Glued. Each molecule of the EB1 dimer contains two helices forming a conserved four-helix bundle, while also providing p150Glued binding sites in its flexible tail region. Combining crystallography, NMR, and mutational analyses, our studies reveal the critical interacting elements of both EB1 and p150Glued, whose mutation alters microtubule polymerization activity. Moreover, removal of the key flexible tail from EB1 activates microtubule assembly by EB1 alone, suggesting that the flexible tail negatively regulates EB1 activity. We, therefore, propose that EB1 possesses an auto-inhibited conformation, which is relieved by p150Glued as an allosteric activator.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Hayashi I,Wilde A,Mal TK,Ikura M

doi

10.1016/j.molcel.2005.06.034

subject

Has Abstract

pub_date

2005-08-19 00:00:00

pages

449-60

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(05)01441-3

journal_volume

19

pub_type

杂志文章

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