Abstract

Eukaryotic protein degradation by the proteasome and the lysosome is a dynamic and complex process in which ubiquitin has a key regulatory role. The distinctive morphology of the postmitotic neuron creates unique challenges for protein degradation systems with respect to cell-surface protein turnover and substrate delivery to proteolytic machineries that are required for both synaptic plasticity and self-renewal. Moreover, the discovery of ubiquitin-positive protein aggregates in a wide spectrum of neurodegenerative diseases underlines the importance and vulnerability of the degradative system in neurons. In this article, we discuss the molecular mechanism of protein degradation in the neuron with respect to both its function and its dysfunction.

Author affiliations

1. Division of Chemistry of Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
2. Division of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125, USA.

Correspondence to: Erin M. Schuman² Email: schumane@caltech.edu

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