Abstract
Here we report that the microtubule-associated proteins MAP2 and tau share two separable functional domains. One is the microtubule-binding site which serves to nucleate microtubule assembly; the second is a short C-terminal alpha-helical sequence which can crosslink microtubules by means of a hydrophobic zipper interaction into dense stable parallel arrays characteristic of axons or dendrites. Thus, interactions between molecules of a single type are capable of drastically reorganizing microtubules and completely suppressing their dynamic properties.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Axons / ultrastructure*
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Binding Sites
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Cell Line
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Cricetinae
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Dendrites / ultrastructure*
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Fluorescent Antibody Technique
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Intermediate Filaments / ultrastructure
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Leucine
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Mice
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Microscopy, Electron
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Microtubule-Associated Proteins / physiology*
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Microtubule-Associated Proteins / ultrastructure
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Microtubules / ultrastructure*
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Protein Conformation
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Structure-Activity Relationship
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tau Proteins
Substances
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Microtubule-Associated Proteins
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tau Proteins
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Leucine