UCL  IRIS
Institutional Research Information Service
UCL Logo
Please report any queries concerning the funding data grouped in the sections named "Externally Awarded" or "Internally Disbursed" (shown on the profile page) to your Research Finance Administrator. Your can find your Research Finance Administrator at https://www.ucl.ac.uk/finance/research/rs-contacts.php by entering your department
Please report any queries concerning the student data shown on the profile page to:

Email: portico-services@ucl.ac.uk

Help Desk: http://www.ucl.ac.uk/ras/portico/helpdesk
Publication Detail
A novel tau mutation in exon 9 (1260V) causes a four-repeat tauopathy.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Grover A, England E, Baker M, Sahara N, Adamson J, Granger B, Houlden H, Passant U, Yen S-H, DeTure M, Hutton M
  • Publication date:
    11/2003
  • Pagination:
    131, 140
  • Journal:
    Exp Neurol
  • Volume:
    184
  • Issue:
    1
  • Status:
    Published
  • Country:
    United States
  • Print ISSN:
    0014-4886
  • PII:
    S0014488603003935
  • Language:
    eng
  • Keywords:
    Aged, Amino Acid Sequence, DNA, Dementia, Exons, Frontal Lobe, Heparin, Humans, Immunohistochemistry, Microtubules, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Phenotype, Reverse Transcriptase Polymerase Chain Reaction, Temporal Lobe, tau Proteins
Abstract
A novel mutation in exon 9 of tau, I260V, is associated with a clinical syndrome consistent with frontotemporal dementia with extensive tau pathology; however, neurofibrillary tangles and Pick bodies are absent. Significantly, Sarkosyl-insoluble tau extracted from affected brain tissue consisted almost exclusively of four-repeat isoforms. Consistent with these findings, in vitro biochemical assays demonstrated that the I260V mutation causes a selective increase in tau aggregation and a decrease in tau-induced microtubule assembly with four-repeat isoforms only. The contrasting pathology and biochemical effects of this mutation suggest a different disease mechanism from the other exon 9 mutations and demonstrates the critical role for the first microtubule-binding domain in tau-promoted microtubule assembly and the pathogenic aggregation of tau.
Publication data is maintained in RPS. Visit https://rps.ucl.ac.uk
 More search options
UCL Researchers
Author
Department of Neuromuscular Diseases
University College London - Gower Street - London - WC1E 6BT Tel:+44 (0)20 7679 2000

© UCL 1999–2011

Search by