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Published online 22 October 2001. doi:10.1083/jcb.200106123
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© The Rockefeller University Press, 0021-9525/2001/10/355 $5.00
The Journal of Cell Biology, Volume 155, Number 3, October 29, 2001 355-368

Article

 Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding

Shilpa Vashist1, Woong Kim1, William J. Belden2, Eric D. Spear1, Charles Barlowe2 and Davis T.W. Ng1

1 Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
2 Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755

Address correspondence to Davis Ng, Dept. of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802. Tel.: (814) 863-5686. Fax: (814) 863-5876. E-mail: dtn1{at}psu.edu

Proteins destined for the secretory pathway must first fold and assemble in the lumen of endoplasmic reticulum (ER). The pathway maintains a quality control mechanism to assure that aberrantly processed proteins are not delivered to their sites of function. As part of this mechanism, misfolded proteins are returned to the cytosol via the ER protein translocation pore where they are ubiquitinated and degraded by the 26S proteasome. Previously, little was known regarding the recognition and targeting of proteins before degradation. By tracking the fate of several mutant proteins subject to quality control, we demonstrate the existence of two distinct sorting mechanisms. In the ER, substrates are either sorted for retention in the ER or are transported to the Golgi apparatus via COPII–coated vesicles. Proteins transported to the Golgi are retrieved to the ER via the retrograde transport system. Ultimately, both retained and retrieved proteins converge at a common machinery at the ER for degradation. Furthermore, we report the identification of a gene playing a novel role specific to the retrieval pathway. The gene, BST1, is required for the transport of misfolded proteins to the Golgi, although dispensable for the transport of many normal cargo proteins.

Key Words: endoplasmic reticulum; vesicular transport; protein degradation; misfolded proteins; glycosylation


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