Tau protein

Tau is a microtubule-associated protein that helps organize neuronal microtubules. Abnormally modified tau can detach from microtubules and aggregate into neurofibrillary tangles.

Microtubule: A hollow cytoskeletal tube built from tubulin that supports cell structure and intracellular transport. Tau binds along neuronal microtubules and helps regulate their stability.
MAPT: The gene that encodes tau protein in humans. Different MAPT transcripts produce tau isoforms with distinct microtubule-binding regions.
Tau PET imaging: Positron emission tomography using tracers designed to detect aggregated tau in the brain. It allows researchers to map tau pathology in living brains.
Amyloid beta: Peptides derived from amyloid precursor protein that can aggregate into plaques in the brain. Amyloid plaques are a second defining Alzheimer pathology, distinct from intracellular tau tangles.
Tau phosphorylation: The addition of phosphate groups to tau, a modification that regulates its interactions and behavior. Excessive phosphorylation can weaken tau’s attachment to microtubules.
Alternative splicing: RNA processing that joins selected exons to produce different messenger RNAs from one gene. Alternative splicing of MAPT generates the major tau isoforms.
Cerebrospinal fluid: The clear fluid that surrounds the brain and spinal cord. Tau concentrations and forms in this fluid can serve as disease biomarkers.
Alpha-synuclein: A neuronal protein that can aggregate into Lewy bodies in Parkinson disease and related disorders. Its aggregation defines synucleinopathies, unlike tauopathies.
Neurofibrillary tangle: An intracellular aggregate of misfolded tau filaments found in several neurodegenerative diseases. These tangles are a characteristic endpoint of pathological tau aggregation.
Tau isoforms: Distinct tau protein forms produced mainly by alternative splicing of MAPT transcripts. Their differing repeat domains affect microtubule binding and disease-associated patterns.

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