Microtubule-associated protein 8 contains two microtubule binding sites

Biochem Biophys Res Commun. 2006 Jan 6;339(1):172-9. doi: 10.1016/j.bbrc.2005.10.199. Epub 2005 Nov 10.


Microtubule-associated proteins (MAPs) are critical regulators of microtubule dynamics and functions, and have long been proposed to be essential for many cellular events including neuronal morphogenesis and functional maintenance. In this study, we report the characterization of a new microtubule-associated protein, we named MAP8. The protein of MAP8 is mainly restricted to the nervous system postnatally in mouse. Its expression could first be detected as early as at embryonic day 10, levels plateau during late embryonic and neonatal periods, and subsequently decrease moderately to remain constant into adulthood. In addition to its carboxyl terminal binding site, the MAP8 polyprotein also contains a functional microtubule-binding domain at its N-terminal segment. The association of the carboxyl terminal of the light chain with actin microfilaments could also be detected. Our findings define MAP8 as a novel microtubule associated protein containing two microtubule binding domains.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Animals
  • Animals, Newborn
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • Mice
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / metabolism*
  • Nervous System / embryology
  • Nervous System / growth & development
  • Nervous System / metabolism
  • Organ Specificity
  • Protein Structure, Tertiary


  • Microtubule-Associated Proteins