Autosomal Recessive Juvenile Parkinson's (AR-JP) is a debilitating disease caused by loss of functions in the parkin gene. The parkin protein normally functions as an E3 ligase in the ubiquitination pathway, a cellular process that facilitates the degradation of misfolded proteins. A loss of parkin function results in the accumulation and aggregation of these misfolded proteins, causing cell death of dopaminergic neurons in patients' brains. It has been recently shown that parkin is directly associated with Nrdp1, another ubiquitin E3 ligase. Further evidence indicates that Nrdp1 promotes parkin degradation and modulates parkin's activities on its substrates. We hypothesize that the regulation of interactions between parkin and Nrdp1 may affect the pathogenesis of PD. In this MQP, a yeast two hybrid approach was used to identify the domain(s) of Nrdp1 that binds parkin. Our long term goal is to design peptides against parkin-binding domain(s) in Nrdp1 so that interactions between these two proteins may be intervened. These peptides would have potential therapeutic uses.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Ehnstrom, James Thomas
• Papaargjir, Ilda

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042605-180601

Advisor

• Adams, David S.

Year

• 2005

Sponsor

• University of Massachusetts Medical School

Date created

• 2005-04-26

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright