Beta Amyloid Peptide: Research Paper : The Dual Roles of Clusterin in Extracellular and Intracellular Proteostasis

The Dual Roles of Clusterin in Extracellular and Intracellular Proteostasis

Abstract

Clusterin (CLU) was the first reported secreted mammalian chaperone and impacts on serious diseases associated with inappropriate extracellular protein aggregation. Many studies have described intracellular CLU in locations outside the secretory system and recent work has shown that CLU can be released into the cytosol during cell stress. In this article, we critically evaluate evidence relevant to the proposed origins of cellular CLU found outside the secretory system, and advance the hypothesis that the cytosolic release of CLU induced by stress serves to facilitate the trafficking of misfolded proteins to the proteasome and autophagy for degradation. We also propose future research directions that could help establish CLU as a unique chaperone performing critical and synergic roles in both intracellular and extracellular proteostasis.

Keywords: autophagy; chaperone; clusterin; misfolded proteins; neurodegenerative diseases; proteasome; proteostasis.

This article originally appeared in the "https://pubmed.ncbi.nlm.nih.gov/33573881/" and has their copyrights. We do not claim copyright on the content. This information is for research purposes only. This Blog is made available by publishers for educational purposes only as well as to give you general information and a general understanding , not to provide specific advice. By using this blog site you understand that there is no client relationship between you and the Blog publisher. The Blog should not be used as a substitute for competent research advice.