The molecular and cellular biology of tau.
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).
Kosik
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Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115.
D000818:Animals; D006801:Humans; D015394:Molecular Structure; D009474:Neurons / Q000737:chemistry; D010766:Phosphorylation; D016875:tau Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology
D016875:tau Proteins