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SNIPER Peptide-Mediated Degradation
of Endogenous Proteins
Xuelai Fan1 and Yu Tian Wang1,2
1Brain Research Centre and Department of Medicine, Vancouver Coastal Health Research
Institute, University of British Columbia, Vancouver, British Columbia, Canada
2Translational Medicine Research Center, China Medical University Hospital, Taichung,
Taiwan
Rapid and reversible methods for altering the function of endogenous proteins
are not only indispensable tools for probing complex biological systems, but
may potentially drive the development of new therapeutics for the treatment of
human diseases. Genetic approaches have provided insights into protein func-
tion, but are limited in speed, reversibility and spatiotemporal control. To over-
come these limitations, we have developed a peptide-based method (SNIPER:
Selective Native Protein Eradication) to degrade any given endogenous protein
at the post-translational level by harnessing chaperone-mediated autophagy, a
major intracellular protein degradation pathway. This unit presents a typical
strategy in the design and validation of a protein-knockdown peptide. C? 2015
by John Wiley Sons, Inc.
Keywords: peptide lysosome protein knockdown chaperone-mediated
autophagy
How to cite this article:
Fan, X. and Wang, Y.T. 2015. SNIPER Peptide-Mediated
Degradation of Endogenous Proteins. Curr. Protoc. Chem. Biol.
7:1-16.
doi: 10.1002/9780470559277.ch140202
INTRODUCTION
Protein Knockdown at the Post-Translational Level
A major challenge in the post-genomic age is to elucidate the function of gene products
in health and disease. A common approach in biomedical research to interrogate protein
function is to use loss-of-function studies, that is, to examine phenotypes developed in
the absence of the protein-of-interest. In this regard, classical gene-knockout approaches
and small interference RNAs (siRNAs) have become powerful tools to interrogate protein
function. While immensely useful, these techniques require manipulation of t
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