Protein Folding and Quality Control in the ER | Zendy

Kazutaka Araki | Zendy; K. Nagata | Zendy

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Protein Folding and Quality Control in the ER

Author(s) -

Kazutaka Araki,

K. Nagata

Publication year - 2012

Publication title -

cold spring harbor perspectives in biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.011

H-Index - 173

ISSN - 1943-0264

DOI - 10.1101/cshperspect.a015438

Subject(s) - biology , protein folding , folding (dsp implementation) , protein quality , quality (philosophy) , control (management) , computational biology , microbiology and biotechnology , biochemistry , computer science , engineering , philosophy , epistemology , artificial intelligence , electrical engineering

The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER quality control (ERQC) system. The ERQC facilitates folding and modification of secretory and membrane proteins and eliminates terminally misfolded polypeptides through ER-associated degradation (ERAD) or autophagic degradation. This mechanism of ER protein surveillance is closely linked to redox and calcium homeostasis in the ER, whose balance is presumed to be regulated by a specific cellular compartment. The potential to modulate proteostasis and metabolism with chemical compounds or targeted siRNAs may offer an ideal option for the treatment of disease.

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