Having trouble accessing articles? Reset your cache.

Aggregation party in ALS

Aggregation and mislocalization of TDP-43 are at the heart of amyotrophic lateral sclerosis, but it is difficult to manipulate the proteindirectly because of its broad role in cellular survival. University of Pennsylvania researchers now have found evidence that TDP-43 interacts with ataxin 2, an intracellular protein linked to another neurodegenerative disease, spinocerebellar ataxia, and think that inhibiting ataxin 2 activitycould provide a handle for preventing the toxicity caused by mislocalized TDP-43.1

Mutations in TAR DNA binding protein 43 (TDP-43; TARDBP) lead to certain rare cases of hereditary amyotrophic lateral sclerosis (ALS), and in a majority of ALS patients the normally soluble protein mislocalizes into aggregates.2 But tinkering with TDP-43 levels can disrupt neurological development, complicating efforts to study the protein's function in mice.

A team led by Aaron Gitler, assistant professor of cell and developmental biology at the University of Pennsylvania, chose a simpler approach to

Read the full 1441 word article

User Sign In

Trial Subscription

Get a two-week free trial subscription to BioCentury

SIGN UP

Article Purchase

This article may not be distributed to non-subscribers
More Info >PURCHASE