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Tau Structures

Open access
Avila, Jesus, Jiménez, Juan S., Sayas, Carmen L., Bolós, Marta, Zabala, Juan C., Rivas, Germán, Hernández, Felix·2016·Frontiers in Aging Neuroscience
DOI 10.3389/fnagi.2016.00262PMC PMC5099159
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Abstract

Tau is a microtubule-associated protein that plays an important role in axonal stabilization, neuronal development, and neuronal polarity. In this review, we focus on the primary, secondary, tertiary, and quaternary tau structures. We describe the structure of tau from its specific residues until its conformation in dimers, oligomers, and larger polymers in physiological and pathological situations.

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Crossref · 10.3389/fnagi.2016.00262

Cites

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Figures

Figure 1 Tau residues and tau regions. (A) The localization in tau molecules of some tau residues is shown. (B) The different tau regions, including the microtubule binding repeats are shown. (C) Intramolecular interactions, like that described for “paper-clip” structure (see text and reference, Jeganathan et al., 2006) could prevent the tau self-interaction by masking the region(s) involved in that interaction.
Figure 1 Tau residues and tau regions. (A) The localization in tau molecules of some tau residues is shown. (B) The different tau regions, including the microtubule binding repeats are shown. (C) Intramolecular interactions, like that described for “paper-clip” structure (see text and reference, Jeganathan et al., 2006) could prevent the tau self-interaction by masking the region(s) involved in that interaction.CC BY · PubMed Central
Figure 2 Interaction tau-tau. Tau protein could be found as an extended common long protein that could bind to other proteins, including itself, in this extended fashion (Hirokawa et al., 1988). The Figure shows how two tau molecules could interact, in an antiparallel fashion, through their microtubule-binding domain where cysteine residues are present.
Figure 2 Interaction tau-tau. Tau protein could be found as an extended common long protein that could bind to other proteins, including itself, in this extended fashion (Hirokawa et al., 1988). The Figure shows how two tau molecules could interact, in an antiparallel fashion, through their microtubule-binding domain where cysteine residues are present.CC BY · PubMed Central
Figure 3 Hypothetical tau circular-like structure. (A) Tau granule (circular-like) structures have been previously reported (Rábano et al., 2013; Takashima, 2013). In the Figure, it is shown an hypothetical closed structure playing with parallel and antiparallel tau molecules. In that structure, a hole in the center surrounded by C-terminal sequences of tau molecule can be found. Since tau C-terminal sequences contain several acidic residues, it is possible the reaction of those residues with metals. It may take place in argylophylic grains. (B) A 3D-like image of the structure is shown. In that image parallel and antiparallel forms, with the C-terminal (blue) or N-terminal (violet), regions of tau molecule at the surface, could be present. It is proposed that those having the C-terminal inside the structure could react with cations.
Figure 3 Hypothetical tau circular-like structure. (A) Tau granule (circular-like) structures have been previously reported (Rábano et al., 2013; Takashima, 2013). In the Figure, it is shown an hypothetical closed structure playing with parallel and antiparallel tau molecules. In that structure, a hole in the center surrounded by C-terminal sequences of tau molecule can be found. Since tau C-terminal sequences contain several acidic residues, it is possible the reaction of those residues with metals. It may take place in argylophylic grains. (B) A 3D-like image of the structure is shown. In that image parallel and antiparallel forms, with the C-terminal (blue) or N-terminal (violet), regions of tau molecule at the surface, could be present. It is proposed that those having the C-terminal inside the structure could react with cations.CC BY · PubMed Central

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  1. Avila, 2012, Threonine localization in a protein molecule, 277

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Metadata

Authors
Avila, J., Jiménez, J. S., Sayas, C. L., Bolós, M., Zabala, J. C., Rivas, G., & Hernández, F.
Affiliations
  • Universidad Autónoma de Madrid (ES)
  • Universidad de La Laguna (ES)
  • Consejo Superior de Investigaciones Científicas (ES)
  • Universidad de Cantabria (ES)
ORCID
Venue
Frontiers in Aging Neuroscience
Publisher
Frontiers Media SA
Published
2016-11-08
Volume
8
Pages
262-262
ISSN
1663-4365 (ISSN-L)
DOI
10.3389/fnagi.2016.00262
PMC
PMC5099159
OpenAlex
W4211132017
Cited by
140
References
122
Citations by year
2026: 11 · 2025: 19 · 2024: 17 · 2023: 22 · 2022: 14 · 2021: 16 · 2020: 12 · 2019: 15 · 2018: 11 · 2017: 2
FWCI
1.09
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Frontiers in Aging Neuroscience (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion)
  • LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (acceptedVersion, other-oa)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • UCrea (University of Cantabria) (submittedVersion, cc-by)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
tau protein, protein structure, microtubule-associated proteins, neuronal polarity, tau oligomers, tauopathy, protein conformation

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