Literature DB >> 11756436

Functional characterization of FTDP-17 tau gene mutations through their effects on Xenopus oocyte maturation.

Patrice Delobel1, Stéphane Flament, Malika Hamdane, Ross Jakes, Arlette Rousseau, André Delacourte, Jean-Pierre Vilain, Michel Goedert, Luc Buée.   

Abstract

tau gene mutations cause frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Here we have used Xenopus oocyte maturation as an indicator of microtubule function. We show that wild-type four-repeat Tau protein inhibits maturation in a concentration-dependent manner, whereas three-repeat Tau has no effect. Of the seven four-repeat Tau proteins with FTDP-17 mutations tested, five (G272V, DeltaK280, P301L, P301S, and V337M) failed to interfere significantly with oocyte maturation, demonstrating a greatly reduced ability to interact with microtubules. One mutant protein (R406W) almost behaved like wild-type Tau, and one (S305N) inhibited maturation more strongly than wild-type Tau. With the exception of R406W, wild-type Tau and all the mutants studied were similarly phosphorylated during the Xenopus oocyte maturation, and this was independent of their effects on this process. Data obtained with R406W and S305N may be related to charge changes (phosphorylation and basic amino acids). Our results demonstrate variable effects of FTDP-17 mutations on microtubules in an intact cell situation. Those findings establish Xenopus oocyte maturation as a system allowing the study of the functional effects of tau gene mutations in a quantitative manner.

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Year:  2001        PMID: 11756436     DOI: 10.1074/jbc.M107716200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  11 in total

1.  Combinatorial Tau pseudophosphorylation: markedly different regulatory effects on microtubule assembly and dynamic instability than the sum of the individual parts.

Authors:  Erkan Kiris; Donovan Ventimiglia; Mehmet E Sargin; Michelle R Gaylord; Alphan Altinok; Kenneth Rose; B S Manjunath; Mary Ann Jordan; Leslie Wilson; Stuart C Feinstein
Journal:  J Biol Chem       Date:  2011-02-02       Impact factor: 5.157

2.  MRNA Levels of ACh-Related Enzymes in the Hippocampus of THY-Tau22 Mouse: A Model of Human Tauopathy with No Signs of Motor Disturbance.

Authors:  Beatriz E García-Gómez; Francisco J Fernández-Gómez; Encarnación Muñoz-Delgado; Luc Buée; David Blum; Cecilio J Vidal
Journal:  J Mol Neurosci       Date:  2015-12-23       Impact factor: 3.444

Review 3.  Tau and tauopathies.

Authors:  Gloria Lee; Chad J Leugers
Journal:  Prog Mol Biol Transl Sci       Date:  2012       Impact factor: 3.622

4.  FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions.

Authors:  Benjamin Combs; T Chris Gamblin
Journal:  Biochemistry       Date:  2012-10-18       Impact factor: 3.162

5.  FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an "alternative core" model for normal and pathological Tau action.

Authors:  Adria C LeBoeuf; Sasha F Levy; Michelle Gaylord; Arnab Bhattacharya; Ambuj K Singh; Mary Ann Jordan; Leslie Wilson; Stuart C Feinstein
Journal:  J Biol Chem       Date:  2008-10-21       Impact factor: 5.157

6.  Developmental Expression of 4-Repeat-Tau Induces Neuronal Aneuploidy in Drosophila Tauopathy Models.

Authors:  Nicolas Malmanche; Pierre Dourlen; Marc Gistelinck; Florie Demiautte; Nichole Link; Cloé Dupont; Lies Vanden Broeck; Elisabeth Werkmeister; Philippe Amouyel; Antonino Bongiovanni; Hélène Bauderlique; Dieder Moechars; Anne Royou; Hugo J Bellen; Frank Lafont; Patrick Callaerts; Jean-Charles Lambert; Bart Dermaut
Journal:  Sci Rep       Date:  2017-01-23       Impact factor: 4.379

7.  Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects.

Authors:  Pascale Barbier; Orgeta Zejneli; Marlène Martinho; Alessia Lasorsa; Valérie Belle; Caroline Smet-Nocca; Philipp O Tsvetkov; François Devred; Isabelle Landrieu
Journal:  Front Aging Neurosci       Date:  2019-08-07       Impact factor: 5.750

8.  Two-dimensional electrophoresis of tau mutants reveals specific phosphorylation pattern likely linked to early tau conformational changes.

Authors:  Alexis Bretteville; Kunie Ando; Antoine Ghestem; Anne Loyens; Séverine Bégard; Jean-Claude Beauvillain; Nicolas Sergeant; Malika Hamdane; Luc Buée
Journal:  PLoS One       Date:  2009-03-17       Impact factor: 3.240

9.  A novel MAPT mutation, G55R, in a frontotemporal dementia patient leads to altered Tau function.

Authors:  Abhinaya Iyer; Nichole E Lapointe; Krzysztof Zielke; Mariusz Berdynski; Elmer Guzman; Anna Barczak; Małgorzata Chodakowska-Żebrowska; Maria Barcikowska; Stuart Feinstein; Cezary Zekanowski
Journal:  PLoS One       Date:  2013-09-27       Impact factor: 3.240

10.  Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3β.

Authors:  Giulia Povellato; Richard I Tuxworth; Diane P Hanger; Guy Tear
Journal:  Biol Open       Date:  2014-01-15       Impact factor: 2.422

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