A τ Fragment Containing a Repetitive Sequence Induces Bundling of Actin Filaments
Author
dc.contributor.author
Moraga, Daniel M.
Author
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Nuñez, Patricio
Author
dc.contributor.author
Garrido, Jorge
Author
dc.contributor.author
Maccioni Baraona, Ricardo
Admission date
dc.date.accessioned
2019-01-29T14:51:21Z
Available date
dc.date.available
2019-01-29T14:51:21Z
Publication date
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1993
Cita de ítem
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Journal of Neurochemistry, Volumen 61, Issue 3, 2018, Pages 979-986
Identifier
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14714159
Identifier
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00223042
Identifier
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10.1111/j.1471-4159.1993.tb03611.x
Identifier
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https://repositorio.uchile.cl/handle/2250/161001
Abstract
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Abstract: Much indirect evidence suggests that the interconnections of actin microfilaments with the microtubule system are mediated by microtubule‐associated proteins (MAPs). In this study we provide new data to support the interaction of a specific tubulin‐binding domain on τ with actin in vitro. In actin polymerization assays, the synthetic peptide VRSKIGSTENLKHQPGGG, corresponding to the first repetitive sequence of τ protein, increased turbidity at 320 nm in a dose‐dependent fashion. A salient feature of the τ peptide‐induced assembly process is the formation of a large amount of actin filament bundles, as revealed by electron microscopic analysis. An increase in the τ peptide concentration resulted in a proportional increase in the bundling of actin filaments. It is interesting that a gradual decrease of pH within the range 7.6–4.7 resulted in a higher effect of τ peptide in promoting bundles of actin filaments. A similar pH‐dependent effect was observed for τ protein‐induced bun