Vesicle Transport: A New Player in APP Trafficking

Vesicle Transport: A New Player in APP Trafficking

The trafficking of the amyloid precursor protein (APP) is critical for controlling the generation of the toxic A beta peptide that is central to amyloid formation in Alzheimer's disease. A new study reveals a key role for the AP4 adaptor protein complex in the Golgi-to-endosome trafficking of APP.

LRRK2: a problem lurking in vesicle trafficking?

Editor's Note: These short, critical reviews of recent papers in the Journal, written exclusively by graduate students or postdoctoral fellows, are intended to summarize the important findings of the paper and provide additional insight and commentary. For more information on the format and purpose of the Journal Club, please see Review of Piccoli et al. Mutations in leucine-rich repeat kinase ...

APP anterograde transport requires Rab3A GTPase activity for assembly of the transport vesicle.

The amyloid precursor protein (APP) is anterogradely transported by conventional kinesin in a distinct transport vesicle, but both the biochemical composition of such a vesicle and the specific kinesin-1 motor responsible for transport are poorly defined. APP may be sequentially cleaved by beta- and gamma-secretases leading to accumulation of beta-amyloid (Abeta) peptides in brains of Alzheimer...

LRRK2 and vesicle trafficking.

Mutations in LRRK2 (leucine-rich repeat kinase 2) (also known as PARK8 or dardarin) are responsible for the autosomal-dominant form of PD (Parkinson's disease). LRRK2 mutations were found in approximately 3-5% of familial and 1-3% of sporadic PD cases with the highest prevalence (up to 40%) in North Africans and Ashkenazi Jews. To date, mutations in LRRK2 are a major genetic risk factor for fam...

Exercise-Regulated Vesicle Trafficking