Degradation of proteins within the endoplasmic reticulum.
Certain newly synthesized proteins within the endoplasmic reticulum undergo rapid turnover by a non-lysosomal proteolytic pathway. Biochemical and morphological evidence has suggested that these proteins never leave the endoplasmic reticulum before they are degraded. The mechanism(s) for the selective targeting of proteins for degradation within the endoplasmic reticulum is still not understood, but appears to rely on specific structural determinants on the protein substrates. Important cellular functions are likely to be served by this endoplasmic reticulum degradative system, including disposal of abnormal proteins and the selective turnover of metabolically regulated proteins.
Bonifacino
J S
JS
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
Lippincott-Schwartz
J
J
D000818:Animals; D053299:Apolipoprotein B-100; D001055:Apolipoproteins B / Q000378:metabolism; D037263:Asialoglycoprotein Receptor; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006903:Hydroxymethylglutaryl CoA Reductases / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D015394:Molecular Structure; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D011971:Receptors, Immunologic / Q000378:metabolism
D053299:Apolipoprotein B-100; D001055:Apolipoproteins B; D037263:Asialoglycoprotein Receptor; D008565:Membrane Proteins; D010446:Peptide Fragments; D011506:Proteins; D011948:Receptors, Antigen, T-Cell; D011971:Receptors, Immunologic; D006903:Hydroxymethylglutaryl CoA Reductases