Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 362, Issue 2, Pages 312-326Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.07.018
Keywords
tau; Alzheimer's; protein folding; protein aggregation; microtubule associated proteins
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Funding
- NIA NIH HHS [R01 AG025440, R01 AG019391-06, R01 AG025440-01A1, R01 AG019391, AG025440, R37 AG019391] Funding Source: Medline
- NIGMS NIH HHS [GM66354] Funding Source: Medline
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The microtubule-associated protein tau is impacted in neurodegeneration and dementia through its deposition in the form of paired helical filaments in Alzheimer's disease neurofibrillary tangles and through mutations linking it to the autosomal dominant disorder frontotemporal dementia with Parkinsonism. When isolated in solution tau is intrinsically unstructured and does not fold, while the conformation of the protein in the microtubule-bound state remains uncharacterized. Here we show that the repeat region of tau, which has been reported both to mediate tau microtubule interactions and to constitute the proteolysis-resistant core of disease-associated tau aggregates, associates with lipid micelles and vesicles and folds into an ordered structure upon doing so. In addition to providing the first structural insights into a folded state of tau, our results support a role for lipid membranes in mediating tau function and tau pathology. (c) 2006 Elsevier Ltd. All rights reserved.
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