Journal
JOURNAL OF CELL BIOLOGY
Volume 157, Issue 7, Pages 1187-1196Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200201048
Keywords
MAP2; tau; structure; microtubule; cryo-EM
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Funding
- NIA NIH HHS [AG-05131, P50 AG005131] Funding Source: Medline
- NIGMS NIH HHS [R37 GM052468, GM-52468, R01 GM052468] Funding Source: Medline
- NIMH NIH HHS [MH50861, F31 MH012504, R01 MH050861, R29 MH050861, MH-12504] Funding Source: Medline
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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 MAP2c 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 he important for the specific targeting of different repeats to either a or p tubulin. These results provide strong evidence suggesting that MAP2c and tau stabilize microtubules by binding along individual protofilaments, possibly by bridging the tubulin interfaces.
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