Literature DB >> 21746797

Cellular strategies of protein quality control.

Bryan Chen1, Marco Retzlaff, Thomas Roos, Judith Frydman.   

Abstract

Eukaryotic cells must contend with a continuous stream of misfolded proteins that compromise the cellular protein homeostasis balance and jeopardize cell viability. An elaborate network of molecular chaperones and protein degradation factors continually monitor and maintain the integrity of the proteome. Cellular protein quality control relies on three distinct yet interconnected strategies whereby misfolded proteins can either be refolded, degraded, or delivered to distinct quality control compartments that sequester potentially harmful misfolded species. Molecular chaperones play a critical role in determining the fate of misfolded proteins in the cell. Here, we discuss the spatial and temporal organization of cellular quality control strategies and their implications for human diseases linked to protein misfolding and aggregation.

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Year:  2011        PMID: 21746797      PMCID: PMC3140689          DOI: 10.1101/cshperspect.a004374

Source DB:  PubMed          Journal:  Cold Spring Harb Perspect Biol        ISSN: 1943-0264            Impact factor:   10.005


  131 in total

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  180 in total

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2.  Peroxiredoxin chaperone activity is critical for protein homeostasis in zinc-deficient yeast.

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6.  Telling right from wrong in life - cellular quality control.

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7.  TRNA mutations that affect decoding fidelity deregulate development and the proteostasis network in zebrafish.

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