PROSITE documentation PDOC00201 [for PROSITE entry PS00229]

Tau and MAP proteins tubulin-binding repeat signature and profile





Description

Microtubules consist of tubulins as well as a group of additional proteins collectively known as the Microtubule Associated Proteins (MAP). MAP's have been classified into two classes: high molecular weight MAP's and Tau protein. These proteins promote microtubule assembly and stabilize microtubules. The C-terminal region of a subset of these proteins contains three or four tandem repeats of a conserved domain of about thirty amino acid residues which is implicated in tubulin-binding and which seems to have a stiffening effect on microtubules. The proteins currently known to contain such repeats are:

  • Tau [1], from neurones.
  • MAP2 [2], a neuronal member of the high molecular weight MAP's.
  • MAP4 [3], a non-neuronal member of the high molecular weight MAP's. MAP4 is is also expressed in some neurons.

The pattern we developed to detect this repeated region spans the last thirteen residues of the repeated region. We also developed a profile which covers the entire repeat.

Note:

The first repeat of MAP2 is not picked up by the pattern because it has Tyr instead of His in position 8, and Lys instead of Gly in position 11.

Expert(s) to contact by email:

Matus A.

Last update:

May 2010 / Profile added.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

TAU_MAP_1, PS00229; Tau and MAP proteins tubulin-binding repeat signature  (PATTERN)

TAU_MAP_2, PS51491; Tau and MAP proteins tubulin-binding repeat profile  (MATRIX)


References

1AuthorsKosik K.S., Orecchio L.D., Bakalis S., Neve R.L.
TitleDevelopmentally regulated expression of specific tau sequences.
SourceNeuron 2:1389-1397(1989).
PubMed ID2560640

2AuthorsMatus A.
TitleStiff microtubules and neuronal morphology.
SourceTrends Neurosci. 17:19-22(1994).
PubMed ID7511844

3AuthorsChapin S.J., Bulinski J.C.
TitleNon-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of neuronal MAP2 and tau.
SourceJ. Cell Sci. 98:27-36(1991).
PubMed ID1905296



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