Introduction to Tau Proteins
Tau proteins are essential components of nerve cells and play an
important role in preserving the structural integrity of
microtubules14. Microtubules are required for the
intracellular transport and organization of cellular structures.
Alternative splicing of MAPT, which is located on chromosome 17q21.3, is
the primary mechanism by which these proteins are
created14,15. Tau proteins interact with tubulin to
stabilize microtubules and govern their assembly, dynamic activity, and
spatial organization16. These processes are controlled
by the spatial structure of the microtubules. They are especially active
in the distal regions of axons, where they increase microtubule
flexibility by controlling phosphorylation14. This
helps the axons transmit signals more efficiently.
The development of tangled filaments is a characteristic feature of
Alzheimer’s disease (AD), which is caused by the hyperphosphorylation of
tau proteins14,15. These tau tangles are a hallmark of
the etiology of Alzheimer’s disease and contribute to the increasing
neurodegeneration that is characteristic of the condition. All six
isoforms of tau protein are hyperphosphorylated in the brain tissue of
patients diagnosed with Alzheimer’s disease (AD).
Tau proteins can be found in a number of different isoforms, with three
isoforms comprising three binding domains and the other three comprising
four binding domains17. These binding domains make it
easier for tau to engage directly with microtubules, which in turn
stimulates microtubule polymerization and helps maintain the dynamics
under control. In addition, tau proteins have a positive charge, which
causes them to be drawn to microtubules that have a negative charge.
Post-translational changes, including phosphorylation, acetylation,
oxidation, ubiquitination, methylation, glycosylation, and
polyamination, can affect tau protein function18.
Polyamination is a posttranslational process. These alterations can
result in enhanced aggregation of tau proteins and creation of tau
tangles, both of which contribute to the pathogenesis of Alzheimer’s
disease16,18.
Understanding the function of tau proteins and their involvement in
Alzheimer’s disease (AD) is essential for the development of specific
therapeutic techniques that can combat the aberrant aggregation of tau
proteins and alleviate some of the debilitating symptoms of this
neurodegenerative condition. The ongoing research that is being
conducted in this area has promise for expanding our knowledge of
Alzheimer’s disease (AD) and possibly developing novel medicines to
tackle this difficult condition.