Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau

S A Lewis; I E Ivanov; G H Lee; N J Cowan

doi:10.1038/342498a0

Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau

Nature. 1989 Nov 30;342(6249):498-505. doi: 10.1038/342498a0.

Authors

S A Lewis¹, I E Ivanov, G H Lee, N J Cowan

Affiliation

¹ Department of Biochemistry, NYU Medical Center, New York 10016.

PMID: 2511449
DOI: 10.1038/342498a0

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

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Animals
Axons / ultrastructure*
Binding Sites
Cell Line
Cricetinae
Dendrites / ultrastructure*
Fluorescent Antibody Technique
Intermediate Filaments / ultrastructure
Leucine
Mice
Microscopy, Electron
Microtubule-Associated Proteins / physiology*
Microtubule-Associated Proteins / ultrastructure
Microtubules / ultrastructure*
Protein Conformation
Structure-Activity Relationship
tau Proteins

Substances

Microtubule-Associated Proteins
tau Proteins
Leucine