Tau protein

Tau protein is a protein that in humans is encoded by the MAPT gene. It is abundant in the nervous system and is involved in the stabilization of microtubules in the axons of neurons. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation.

Structure

Tau proteins are produced through alternative splicing of a single gene that in humans is designated MAPT (microtubule-associated protein tau). Six tau isoforms exist in brain tissue. These isoforms differ from each other by the presence or absence of one to four repeat domains in the carboxy-terminal half of the molecule. The repeat domains, which are located towards the carboxy terminus of the protein, bind to microtubules and are responsible for the protein's microtubule-binding activity.

Function

Tau proteins are involved in microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The tau proteins, especially in neuronal cells, constantly interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau is absent from the cell body and is present in axons.

Clinical significance

Abnormalities in tau protein function and its interaction with microtubules have been linked to a variety of neurological disorders, including Alzheimer's disease, Pick's disease, and frontotemporal dementia and parkinsonism linked to chromosome 17. In these diseases, tau proteins become hyperphosphorylated, leading to the formation of neurofibrillary tangles and the disintegration of microtubules in brain cells.

Tau protein Resources
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