Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau.
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.
Lewis
S A
SA
Department of Biochemistry, NYU Medical Center, New York 10016.
Ivanov
I E
IE
Lee
G H
GH
Cowan
N J
NJ
D000818:Animals; D001369:Axons / Q000648:ultrastructure*; D001665:Binding Sites; D002460:Cell Line; D006224:Cricetinae; D003712:Dendrites / Q000648:ultrastructure*; D005455:Fluorescent Antibody Technique; D007382:Intermediate Filaments / Q000648:ultrastructure; D007930:Leucine; D051379:Mice; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000502:physiology* / Q000648:ultrastructure; D008870:Microtubules / Q000648:ultrastructure*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D016875:tau Proteins
D008869:Microtubule-Associated Proteins; D016875:tau Proteins; D007930:Leucine