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The Gp78 ubiquitin ligase: probing endoplasmic reticulum complexity

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Abstract

The endoplasmic reticulum (ER) has been classically divided, based on electron microscopy analysis, into parallel ribosome-studded rough ER sheets and a tubular smooth ER network. Recent studies have identified molecular constituents of the ER, the reticulons and DP1, that drive ER tubule formation and whose expression determines expression of ER sheets and tubules and thereby rough and smooth ER. However, segregation of the ER into only two domains remains simplistic and multiple functionally distinct ER domains necessarily exist. In this review, we will discuss the sub-organization of the ER in different domains focusing on the localization and role of the gp78 ubiquitin ligase in the mitochondria-associated smooth ER and on the evidence for a quality control ERAD domain.

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Acknowledgments

Work on this project is supported by a grant from the Canadian Institutes for Health Research (CIHR MT-15132). PSP is the recipient of a CIHR Frederick Banting and Charles Best Canada Graduate Scholarship.

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The authors declare that they have no conflict of interest.

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  1. Department of Cellular and Physiological Sciences, Life Sciences Institute, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada

    Pascal St. Pierre & Ivan R. Nabi

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  1. Pascal St. Pierre
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  2. Ivan R. Nabi
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Correspondence to Ivan R. Nabi.

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St. Pierre, P., Nabi, I.R. The Gp78 ubiquitin ligase: probing endoplasmic reticulum complexity. Protoplasma 249 (Suppl 1), 11–18 (2012). https://doi.org/10.1007/s00709-011-0344-8

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