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Article Addendum

Autophagy of an oxidized, aggregated protein beyond the ER: A pathway for remarkably late-stage quality control

Edward A. Fisher and Kevin Jon Williams

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The authors recently reported a novel role for autophagy in late-stage quality control of a secreted protein, apolipoprotein-B₁₀₀ (apoB). Hepatocytes assemble this protein with triglycerides, cholesterol, and other lipids into macromolecular complexes called lipoproteins. In what appears to be a normal response to diets rich in polyunsaturated fatty acids, which are readily peroxidized, apoB comes into contact with lipid peroxides in or after the Golgi apparatus. The protein becomes oxidatively damaged, aggregates, and is diverted out of the secretory pathway by autophagosomes, which deliver it to lysosomes for destruction. ApoB secretory control via autophagosomes is likely a key component of normal and pathological regulation of plasma lipoprotein levels, as well as a means for remarkably late-stage quality control of a secreted protein.

Addendum to: Pan M, Maitin V, Parathath S, et al. Pre-secretory oxidation, aggregation, and autophagosomal destruction of apolipoprotein-B: A pathway for late-stage quality control. Proc Natl Acad Sci USA 2008; 105:5862-7.

Authors

Edward A. Fisher

NYU School of Medicine

Kevin Jon Williams

Thomas Jefferson University

This is an open-access article

 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.