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Preventing Oligomerization of β-arrestin-2 Improves Clearance of Tau via Autophagy

Preventing Oligomerization of β-arrestin-2 Improves Clearance of Tau via Autophagy
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In today’s research materials, scientists report on the discovery of a maladaptive response to the presence of tau aggregates in brain cells, one that makes the situation worse than it would otherwise be. Tau is one of a small number of proteins that can become altered in a way that ensures other molecules of the same protein also alter. They join together and precipitate into solid structures, known as neurofibrillary tangles in the case of tau, accompanied by a halo of disrupted biochemistry that is harmful to cell and tissue function. This spreads, seeding dysfunction as it moves from cell to cell, or throughout a tissue between cells.

tauneurofibrillary tangles

Cells do attempt to fight back against the spread of broken proteins and their aggregates. Multiple mechanisms allow cells to ingest and break down aggregates present between cells, and aggregates inside cells are also fed into the same recycling machinery. It is perhaps the case that neurodegenerative conditions are age-related in large part because the machinery of autophagy, an important recycling mechanism in cells, degrades with age. The efforts to reduce molecular waste such as protein aggregates falter.

neurodegenerative conditionsautophagyprotein aggregates

Here, researchers have found that an oligomerized form

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Article originally posted at

www.fightaging.org

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