Intracellular trafficking and synaptic function of APL-1 in Caenorhabditis elegans.

ABSTRACT:

Background

Alzheimer's disease (AD) is a neurodegenerative disorder primarily characterized by the deposition of β-amyloid plaques in the brain. Plaques are composed of the amyloid-β peptide derived from cleavage of the amyloid precursor protein (APP). Mutations in APP lead to the development of Familial Alzheimer's Disease (FAD), however, the normal function of this protein has proven elusive. The organism Caenorhabditis elegans is an attractive model as the amyloid precursor-like protein (APL-1) is the single ortholog of APP, and loss of apl-1 leads to a severe molting defect and early larval lethality.

Methodology/principal findings

We report here that lethality and molting can be rescued by full length APL-1, C-terminal mutations as well as a C-terminal truncation, sugge

SUBMITTER: Wiese M 

PROVIDER: S-EPMC2942829 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature