Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). 2005

Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya 464-8602. shuh@biochem.chem.nagoya-u.ac.jp

Secreted proteins are synthesized at the endoplasmic reticulum (ER), and a quality control mechanism in the ER is essential to maintain secretory pathway homeostasis. Newly synthesized soluble and integral membrane secreted proteins fold into their native conformations with the aid of ER molecular chaperones before they are transported to post-ER compartments. However, terminally mis-folded proteins may be retained in the ER and degraded by a process called ER-associated degradation (ERAD). Recent studies using yeast have shown that molecular chaperones both in the ER and in the cytosol play key roles during the ERAD of mis-folded proteins. One important role for chaperones during ERAD is to prevent substrate protein aggregation. Substrate selection is another important role for molecular chaperones during ERAD.

UI MeSH Term Description Entries
D008361 Mannosidases Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE. Mannosidase
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D004721 Endoplasmic Reticulum A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed) Ergastoplasm,Reticulum, Endoplasmic
D017510 Protein Folding Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D018832 Molecular Chaperones A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures. Chaperones, Molecular,Chaperone, Molecular,Molecular Chaperone
D018840 HSP70 Heat-Shock Proteins A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures. Heat-Shock Proteins 70,Heat Shock 70 kDa Protein,Heat-Shock Protein 70,HSP70 Heat Shock Proteins,Heat Shock Protein 70,Heat Shock Proteins 70,Heat-Shock Proteins, HSP70

Related Publications

Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
June 2007, The Biochemical journal,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
August 2012, Current protein & peptide science,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
May 2004, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
January 2013, DNA and cell biology,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
January 2005, Methods in molecular biology (Clifton, N.J.),
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
October 2010, Diabetes, obesity & metabolism,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
January 2005, Methods in molecular biology (Clifton, N.J.),
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
August 2019, Cold Spring Harbor perspectives in biology,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
November 2007, The Journal of biological chemistry,
Shuh-ichi Nishikawa, and Jeffrey L Brodsky, and Kunio Nakatsukasa
August 2018, Planta medica,
Copied contents to your clipboard!