The molecular and cellular biology of tau

Brain Pathol. 1993 Jan;3(1):39-43. doi: 10.1111/j.1750-3639.1993.tb00724.x.


Tau protein was a well-studied molecule before it was discovered in the Alzheimer neurofibrillary tangles. As a microtubule-associated protein (MAP), it continues to be of interest to microtubule biologists who have provided a rather rich knowledge about this protein. Recent work suggests that tau, a neuronal MAP, is capable of generating some features of an axonal shape and an axon-like organization of the cytoskeleton. The importance of tau in pathology stems from its relationship to Alzheimer paired helical filaments and dystrophic neurites. Tau was first believed to be a component of paired helical filaments based upon immunocytochemical grounds (1-6) and then conclusively demonstrated by protein chemical techniques (7-9). Most recently it was shown that bacterially expressed tau fragments from the microtubule-binding domain can self-assemble into paired helical filaments that resemble those from the Alzheimer brain (10).

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Molecular Structure
  • Neurons / chemistry
  • Phosphorylation
  • tau Proteins* / analysis
  • tau Proteins* / chemistry
  • tau Proteins* / genetics
  • tau Proteins* / metabolism
  • tau Proteins* / physiology


  • tau Proteins