Microtubule-associated protein

MAPs bind to the tubulin subunits that make up microtubules to regulate their stability.

A large variety of MAPs have been identified in many different cell types, and they have been found to carry out a wide range of functions.

Thus, the hyperphosphorylation of tau leads to massive detachment, which in turn greatly reduces the stability of microtubules in nerve cells.

[9] This increase in microtubule instability may be one of the main causes of the symptoms of Alzheimer's disease.

Type II MAPs are found exclusively in nerve cells in mammals.

Tau has the additional function of facilitating bundling of microtubules within the nerve cell.

Thus, the hyperphosphorylation of tau leads to massive detachment, which in turn greatly reduces the stability of microtubules in nerve cells.

[6] This increase in microtubule instability may be one of the main causes of the symptoms of Alzheimer's disease.

[2] Male mice lacking MAPS function experience pachytene arrest and spermatocyte death leading to infertility.

[2] MAPS mutant spermatocytes arrested at early pachytene show defects in DNA double-strand break repair.

In addition, plus end tracking proteins, which bind to the very tip of growing microtubules, have also been identified.

During mitosis the dynamic instability of microtubules has been observed to rise approximately tenfold.

This is partly due to phosphorylation of XMAP215, which makes catastrophes (rapid depolymerization of microtubules) more likely.

Certain motor proteins were originally designated as MAPs before it was found that they utilized ATP hydrolysis to transport cargo.