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Quality control of protein folding in extracellular space

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posted on 2024-11-14, 15:32 authored by Justin Yerbury, Elise M Stewart, A R Wyatt, Mark WilsonMark Wilson
The pathologies of many serious human diseases are thought to develop from the effects of intra- or extracellular aggregates of non-native proteins. Inside cells, chaperone and protease systems regulate protein folding; however, little is known about any corresponding mechanisms that operate extracellularly. The identification of these mechanisms is important for the development of new disease therapies. This review briefly discusses the consequences of protein misfolding, the intracellular mechanisms that control folding and the potential corresponding extracellular control processes. Finally, a new speculative model is described, which proposes that newly discovered extracellular chaperones bind to exposed regions of hydrophobicity on non-native, extracellular proteins to target them for receptor-mediated endocytosis and intracellular, lysosomal degradation.

History

Citation

This article was originally published as Yerbury, JJ, Stewart, EM, Wyatt, AR and Wilson, MR, Quality control of protein folding in extracellular space, EMBO Reports, 6 (12), 2005, 1131-1136. Copyright Nature Publishing Group. Original article available here.

Journal title

EMBO Reports

Volume

6

Issue

12

Pagination

1131-1136

Language

English

RIS ID

13219

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