Cited by 929Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroinflammation and Neurodegeneration Mechanisms

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

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Goedert, M., Jakes, R.·1990·The EMBO Journal

DOI 10.1002/j.1460-2075.1990.tb07870.xPMC PMC552204

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Abstract

We have expressed six previously cloned isoforms of human microtubule-associated tau protein in Escherichia coli and purified them to homogeneity in a biologically active form. They range from 352 to 441 amino acids in length and differ from each other by the presence of three or four tandem repeats in the carboxy-terminal half and by the presence or absence of 29 or 58 amino acid inserts in the amino-terminus. When mixed together they gave a set of six bands on SDS-PAGE gels with apparent molecular weights of 48-67 kd and with a characteristic pattern of spacings. Four of these bands aligned with the major tau bands found in adult human cerebral cortex following perchloric acid extraction and alkaline phosphatase treatment. They consisted of isoforms with three repeats and no insertions, four repeats and no amino-terminal insertions and three- and four-repeat containing isoforms with the 29 amino acid insertion. In fetal human brain extracts treated with alkaline phosphatase one of the two major tau bands aligned with the three-repeat containing isoform with no insertions, whereas the molecular nature of the second major tau band remains to be established. The recombinant tau isoforms were biologically active at micromolar concentrations, as assessed by their ability to promote microtubule assembly. The rates of assembly were 2.5-3.0 times faster for isoforms containing four repeats when compared with three-repeat containing isoforms, with no significant contribution by the amino-terminal insertions.

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“(1990) [58].”
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BackgroundMethodSelf-citation
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“Tau-4R isoforms promote microtubule assembly at a faster rate than the tau-3R isoforms (Goedert and Jakes, 1990), suggesting that tau-3R protein may aid newborn neurons to differentiate www.frontiersin.org July 2012 | Volume 6 | Article 104 | 3 by decreasing microtubule stability.”
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Human tau protein forms complex with PrP and some GSS- and fCJD-related PrP mutants possess stronger binding activities with tau in vitro
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“Since the 4R tau isoforms contain an extra MT-binding repeat R2, they show higher affinity with MTs than the 3R isoforms (Goedert and Jakes 1990).”
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Interactions between Tau and Different Conformations of Tubulin: Implications for Tau Function and Mechanism
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Tau Phosphorylation and Cleavage in Ethanol-Induced Neurodegeneration in the Developing Mouse Brain
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BackgroundInfluential
Hierarchical Phosphorylation of Recombinant Tau by the Paired‐Helical Filament‐Associated Protein Kinase Is Dependent on Cyclic AMP‐Dependent Protein Kinase
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“…in this region of the tau molecule composing the fourth microtubule binding repeat have been shown to influence the association between tau and microtubule arrays (Goedert and Jakes, 1990; Drechsel et al., 1992; Raffaelli et al., 1992; Biernat et al., 1993; for review, see Lee, 1993).”
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Enhancing Top-Down Proteomics of Brain Tissue with FAIMS
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An immunochemical study on tau glycation in paired helical filaments
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The Slow Axonal Transport of the Microtubule-Associated Protein Tau and the Transport Rates of Different Isoforms and Mutants in Cultured Neurons
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Authors: Goedert, M., & Jakes, R.
Affiliations: MRC Laboratory of Molecular Biology (GB)
ORCID: Goedert, M.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1990-12-01
Volume: 9
Issue: 13
Pages: 4225-4230
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1990.tb07870.x
PMC: PMC552204
OpenAlex: W1509571186
Cited by: 929
References: 46
Citations by year: 2026: 23 · 2025: 29 · 2024: 50 · 2023: 39 · 2022: 40 · 2021: 53 · 2020: 34 · 2019: 39 · 2018: 42 · 2017: 41 · 2016: 27 · 2015: 37 · 2014: 18 · 2013: 21 · 2012: 25
FWCI: 15.03
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tau protein, tau isoforms, microtubule-associated proteins, microtubule assembly, tandem repeats, recombinant protein expression, cerebral cortex, fetal brain
MeSH terms: Aged, Alkaline Phosphatase, Alzheimer Disease, Amino Acid Sequence, Brain, Escherichia coli, Humans, Isomerism, Microtubule-Associated Proteins, Middle Aged, Molecular Sequence Data, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, RNA Splicing, RNA, Messenger, Tubulin, Mutagenesis, Site-Directed, tau Proteins

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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

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