Faculty Advisor

Adams, David S.

Center

Worcester, MA

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2005

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

Project Center

Worcester, MA

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