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Map2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

Academic Article
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Overview

related to degree

  • Al-Bassam, Jawdat, Ph.D. in Molecular and Cellular Structure and Chemistry, Scripps Research 1998 - 2003
  • Ozer, Rachel Susan, Ph.D. in Chemistry, Scripps Research 1995 - 2001

authors

  • Al-Bassam, Jawdat
  • Ozer, Rachel Susan
  • Safer, D.
  • Halpain, Shelley
  • Milligan, Ronald

publication date

  • June 2002

journal

  • Journal of Cell Biology  Journal

abstract

  • MAP2 and tau exhibit microtubule-stabilizing activities that are implicated in the development and maintenance of neuronal axons and dendrites. The proteins share a homologous COOH-terminal domain, composed of three or four microtubule binding repeats separated by inter-repeats (IRs). To investigate how MAP2 and tau stabilize microtubules, we calculated 3D maps of microtubules fully decorated with MAP2c or tau using cryo-EM and helical image analysis. Comparing these maps with an undecorated microtubule map revealed additional densities along protofilament ridges on the microtubule exterior, indicating that MAP2c and tau form an ordered structure when they bind microtubules. Localization of undecagold attached to the second IR of MAP2c showed that IRs also lie along the ridges, not between protofilaments. The densities attributable to the microtubule-associated proteins lie in close proximity to helices 11 and 12 and the COOH terminus of tubulin. Our data further suggest that the evolutionarily maintained differences observed in the repeat domain may be important for the specific targeting of different repeats to either alpha or beta tubulin. These results provide strong evidence suggesting that MAP2c and tau stabilize microtubules by binding along individual protofilaments, possibly by bridging the tubulin interfaces.

subject areas

  • Animals
  • Binding Sites
  • Cattle
  • Cytoskeleton
  • Humans
  • Imaging, Three-Dimensional
  • Mice
  • Microtubule-Associated Proteins
  • Microtubules
  • Models, Biological
  • Models, Molecular
  • Mutation
  • Protein Binding
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Tubulin
  • tau Proteins
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Research

keywords

  • MAP2
  • cryo-EM
  • microtubule
  • structure
  • tau
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Identity

PubMed Central ID

  • PMC2173547

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200201048

PubMed ID

  • 12082079
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Additional Document Info

start page

  • 1187

end page

  • 1196

volume

  • 157

issue

  • 7

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