Tau protein binds to microtubules through a flexible array of distributed weak sites - PubMed (original) (raw)
Comparative Study
Tau protein binds to microtubules through a flexible array of distributed weak sites
K A Butner et al. J Cell Biol. 1991 Nov.
Abstract
Tau protein plays a role in the extension and maintenance of neuronal processes through a direct association with microtubules. To characterize the nature of this association, we have synthesized a collection of tau protein fragments and studied their binding properties. The relatively weak affinity of tau protein for microtubules (approximately 10(-7) M) is concentrated in a large region containing three or four 18 amino acid repeated binding elements. These are separated by apparently flexible but less conserved linker sequences of 13-14 amino acids that do not bind. Within the repeats, the binding energy for microtubules is delocalized and derives from a series of weak interactions contributed by small groups of amino acids. These unusual characteristics suggest tau protein can assume multiple conformations and can pivot and perhaps migrate on the surface of the microtubule. The flexible structure of the tau protein binding interaction may allow it to be easily displaced from the microtubule lattice and may have important consequences for its function.
Similar articles
- Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau.
Goode BL, Feinstein SC. Goode BL, et al. J Cell Biol. 1994 Mar;124(5):769-82. doi: 10.1083/jcb.124.5.769. J Cell Biol. 1994. PMID: 8120098 Free PMC article. - Repeat motifs of tau bind to the insides of microtubules in the absence of taxol.
Kar S, Fan J, Smith MJ, Goedert M, Amos LA. Kar S, et al. EMBO J. 2003 Jan 2;22(1):70-7. doi: 10.1093/emboj/cdg001. EMBO J. 2003. PMID: 12505985 Free PMC article. - Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau.
Panda D, Goode BL, Feinstein SC, Wilson L. Panda D, et al. Biochemistry. 1995 Sep 5;34(35):11117-27. doi: 10.1021/bi00035a017. Biochemistry. 1995. PMID: 7669769 - First tau repeat domain binding to growing and taxol-stabilized microtubules, and serine 262 residue phosphorylation.
Devred F, Douillard S, Briand C, Peyrot V. Devred F, et al. FEBS Lett. 2002 Jul 17;523(1-3):247-51. doi: 10.1016/s0014-5793(02)02999-x. FEBS Lett. 2002. PMID: 12123840 - Tau Aggregation.
Hernández F, Ferrer I, Pérez M, Zabala JC, Del Rio JA, Avila J. Hernández F, et al. Neuroscience. 2023 May 10;518:64-69. doi: 10.1016/j.neuroscience.2022.04.024. Epub 2022 May 4. Neuroscience. 2023. PMID: 35525497 Review.
Cited by
- Development and characterization of novel anti-acetylated tau monoclonal antibodies to probe pathogenic tau species in Alzheimer's disease.
Bryan Iii MR, Tian X, Tseng JH, Evangelista BA, Ragusa JV, Bryan AF, Trotman W, Irwin D, Cohen TJ. Bryan Iii MR, et al. Acta Neuropathol Commun. 2024 Oct 12;12(1):163. doi: 10.1186/s40478-024-01865-1. Acta Neuropathol Commun. 2024. PMID: 39396065 Free PMC article. - Mixtures of Intrinsically Disordered Neuronal Protein Tau and Anionic Liposomes Reveal Distinct Anionic Liposome-Tau Complexes Coexisting with Tau Liquid-Liquid Phase Separated Coacervates.
Tchounwou C, Jobanputra AJ, Lasher D, Fletcher BJ, Jacinto J, Bhaduri A, Best RL, Fisher WS, Ewert KK, Li Y, Feinstein SC, Safinya CR. Tchounwou C, et al. bioRxiv [Preprint]. 2024 Jul 17:2024.07.15.603342. doi: 10.1101/2024.07.15.603342. bioRxiv. 2024. PMID: 39071287 Free PMC article. Updated. Preprint. - G272V and P301L Mutations Induce Isoform Specific Tau Mislocalization to Dendritic Spines and Synaptic Dysfunctions in Cellular Models of 3R and 4R Tau Frontotemporal Dementia.
Yu K, Yao KR, Aguinaga MA, Choquette JM, Liu C, Wang Y, Liao D. Yu K, et al. J Neurosci. 2024 Jul 10;44(28):e1215232024. doi: 10.1523/JNEUROSCI.1215-23.2024. J Neurosci. 2024. PMID: 38858079 - Transcriptional programs mediating neuronal toxicity and altered glial-neuronal signaling in a Drosophila knock-in tauopathy model.
Bukhari H, Nithianandam V, Battaglia RA, Cicalo A, Sarkar S, Comjean A, Hu Y, Leventhal MJ, Dong X, Feany MB. Bukhari H, et al. Genome Res. 2024 May 15;34(4):590-605. doi: 10.1101/gr.278576.123. Genome Res. 2024. PMID: 38599684 Free PMC article. - Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles.
Kohl PA, Song C, Fletcher BJ, Best RL, Tchounwou C, Garcia Arceo X, Chung PJ, Miller HP, Wilson L, Choi MC, Li Y, Feinstein SC, Safinya CR. Kohl PA, et al. Nat Commun. 2024 Mar 15;15(1):2362. doi: 10.1038/s41467-024-46438-x. Nat Commun. 2024. PMID: 38491006 Free PMC article.
References
- EMBO J. 1988 Jul;7(7):1957-63 - PubMed
- J Cell Biol. 1982 Feb;92(2):435-42 - PubMed
- EMBO J. 1990 Dec;9(13):4225-30 - PubMed
- Proc Natl Acad Sci U S A. 1986 Dec;83(23):9011-5 - PubMed
- Cell. 1985 Sep;42(2):497-505 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases