| Literature References | 1. SPILLANTINI, M.G. AND GOEDERT, M.
Tau protein pathology in neurodegenerative diseases.
TRENDS NEUROSCIENCE 21 428-433 (1998).
2. HARADA, A., OGUCHI, K., OKABE, S., KUNO, J., TERADA, S., OHSHIMA, T.,
SATO-YOSHITAKE, R., TAKEI, Y., NODA, T. AND HIROKAWA, N.
Altered microtubule organization in small-calibre axons of mice lacking
tau protein.
NATURE 369 488-491 (1994).
3. WILHELMSEN, K.C.
The tangled biology of tau.
PROC.NATL.ACAD.SCI.U.S.A. 96 7120-7121 (1999).
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| Documentation | Tau proteins are microtubule-associated proteins that are involved in
microtubule assembly and stabilisation. Tau mRNA is expressed predominantly
in neurones, and particularly in their axons. Quite a number of isoforms
have been detected, which in human brain have been shown to arise from
alternative splicing of an mRNA from a single gene located on chromosome 17.
The isoforms contain 352-441 amino acid residues. A larger tau isoform has
also been detected, which is expressed principally in the peripheral nervous
system [1]. Each isoform contains a variable number of C-terminal repeat
regions that are thought to be responsible for tubulin-binding, and a
variable N-terminal region, whose function remains uncertain.
Tau does not appear to be an essential protein, since transgenic mice
lacking tau appear to develop a normal nervous system with only mild
alterations in the structure of certain small-calibre axons [2]. However,
it has received much recent attention due to its possible role in the
aetiogenesis of a number of human neurodegenerative diseases, filamentous
inclusions containing tau having been found in the brains of patients
diagnosed with Alzheimer's disease, Pick's disease and progressive
supranuclear palsy. Furthermore, tau gene mutations have been found in
patients suffering familial frontotemporal dementia, which result in
abnormal tau protein aggregates forming in the brain tissue [3].
TAUPROTEIN is a 6-element fingerprint that provides a signature for tau
proteins. The fingerprint was derived from an initial alignment of 11
sequences: the motifs were drawn from conserved regions within the
N-terminal half of the alignment - motifs 1-5 lie within the N-terminal
region proximal to the tubulin-binding repeats; and motif 6 spans the end
of the N-terminal region and the start of the first tubulin-binding repeat.
Two iterations on SPTR37_10f were required to reach convergence, at which
point a true set comprising 18 sequences was identified.
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