Tau protein: Difference between revisions

Additionally, tau has a transient secondary structure of α-helices, β-pleated sheets, and a poly-proline II helix <ref name="mandelkow"/>. Tau does not resemble a globular protein, but has characteristics of a denatured, unfolded protein which contributes to its overall hydrophilicity <ref name="schweers">PMID: 7929085</ref>. It can also interact with other tau proteins to form <scene name='71/716561/Tau_aggregation/1'>aggregations</scene>.  

'''Alternative Splicing'''

Alternative splicing of the human tau gene 17q21 generates several isoform structures, which differ by one or two small inserts in its N-terminal region <ref name="Lei">PMID: 20678581</ref>. Although there are 16 exons within the 17q21 gene, exons 4A, 6, and 8 are expressed in peripheral rather than neural tau proteins <ref name="Buee">Buee, L, Bussiere, T, Buee-Scherrer, V, Delacourte, A, Hof, PR. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Rev. 33:95-130 (2000). DOI: 10.1016/S0165-0173(00)00019-9</ref>. Alternatively, eight of the exons (1, 4, 5, 7, 9, 11, 12, and 13) are involved in structural aspects of tau <ref name="Buee"/>. Alternative splicing of exons 2, 3, and 10 is responsible for the 6 isoforms of tau <ref name="Lei"/>. These isoforms differ in 3 or 4 tubulin binding domains within the C-terminal region <ref name="Kolarova"/>.  

Protein aggregation also exists in patients suffering from Parkinson’s disease, specifically within the substantia nigra of the midbrain <ref name="Ross">PMID: 15272267</ref>. Immunohistochemical studies reveal that abnormally phosphorylated tau proteins are partially involved in the development of Lewy bodies, protein aggregates, within the substantia nigra <ref name="Ishizawa">PMID: 12722831</ref>. Lewy bodies may be involved in the neurodegeneration of dopaminergic neurons within this area <ref name="Ross"/>.