2016
DOI: 10.3389/fnagi.2016.00262
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Tau Structures

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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Cited by 100 publications
(92 citation statements)
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References 121 publications
(147 reference statements)
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“…Although tau is considered a natively unfolded protein [sometimes also called an intrinsically disordered protein (IDP)], its ability to adopt various structural states is important to its functions and pathological properties. Since the first report on tau structure in 1977 [38], there have been numerous approaches and reports addressing tau structure in various contexts (reviewed in [39]). While the intrinsically disordered nature of tau precludes the use of crystallographic methods, circular dichroism, nuclear magnetic resonance (NMR) spectroscopy, and more recently cryogenic Location of the projection domain, proline-rich domain, MTBDs, and the parts of tau protein encoded by the alternatively spliced exons 2, 3 and 10 are shown on top of the longest tau isoform (2N4R, 441 aa).…”
Section: Structural Plasticity and Aggregation Of Taumentioning
confidence: 99%
“…Although tau is considered a natively unfolded protein [sometimes also called an intrinsically disordered protein (IDP)], its ability to adopt various structural states is important to its functions and pathological properties. Since the first report on tau structure in 1977 [38], there have been numerous approaches and reports addressing tau structure in various contexts (reviewed in [39]). While the intrinsically disordered nature of tau precludes the use of crystallographic methods, circular dichroism, nuclear magnetic resonance (NMR) spectroscopy, and more recently cryogenic Location of the projection domain, proline-rich domain, MTBDs, and the parts of tau protein encoded by the alternatively spliced exons 2, 3 and 10 are shown on top of the longest tau isoform (2N4R, 441 aa).…”
Section: Structural Plasticity and Aggregation Of Taumentioning
confidence: 99%
“…Under physiological condition, tau exists in an unfolded state, and 80% of the proteins interact with microtubule in neurons [22,26]. When tau is not interacting with other proteins, it may curl on its own, and this random curled state is believed important for preventing interactions with other tau proteins by masking the possible interacting sites [27,28]. The protein itself is bipolar; the N-terminal side is highly negatively charged in normal physiology, while the proline-rich domain and C-terminal end are positively charged, allowing it to interact with the negatively charged C-terminal of tubulins [22,29].…”
Section: Tau Structures and Functionsmentioning
confidence: 99%
“…The six tau isoforms range from 352 to 441 amino acids. Tau isoforms vary in either having zero, one, or two N-terminal inserts (exons 2 and 3) and three or four repeats region at the C-terminal region (exon 10) (10, 11).…”
Section: Introductionmentioning
confidence: 99%