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First published online April 22, 2005; 10.1104/pp.105.060087

Plant Physiology 138:218-231 (2005)
© 2005 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Identification and Characterization of Endoplasmic Reticulum-Associated Degradation Proteins Differentially Affected by Endoplasmic Reticulum Stress1

Mariana E. Kirst, David J. Meyer, Bryan C. Gibbon, Rudolf Jung and Rebecca S. Boston*

Department of Botany, North Carolina State University, Raleigh, North Carolina 27695–7612 (M.E.K., R.S.B.); Pioneer Hi-Bred International, Incorporated, a DuPont Company, Johnston, Iowa 50131 (D.J.M., R.J.); and Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721 (B.C.G.)

The disposal of misfolded proteins from the lumen of the endoplasmic reticulum (ER) is one of the quality control mechanisms present in the protein secretory pathway. Through ER-associated degradation, misfolded substrates are targeted to the cytosol where they are degraded by the proteasome. We have identified four maize (Zea mays) Der1-like genes (Zm Derlins) that encode homologs of Der1p, a yeast (Saccharomyces cerevisiae) protein implicated in ER-associated degradation. Zm Derlins are capable of functionally complementing a yeast Der1 deletion mutant. Such complementation indicates that the Der1p function is conserved among species. Zm Derlin genes are expressed at low levels throughout the plant, but appear prevalent in tissues with high activity of secretory protein accumulation, including developing endosperm cells. Expression of three of the four Zm Derlin genes increases during ER stress, with Zm Derlin1-1 showing the strongest induction. Subcellular fractionation experiments localized Zm Derlin proteins to the membrane fraction of microsomes. In maize endosperm, Zm Derlin proteins were found primarily associated with ER-derived protein bodies regardless of the presence of an ER stress response.

1 This work was supported by the U.S. Department of Energy (grant no. DE–FG02–00ER150065 to R.S.B.), by Pioneer Hi-Bred International, and by the North Carolina Agricultural Research Service (to R.S.B.).

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.060087.

* Corresponding author; e-mail boston{at}unity.ncsu.edu; fax 919–515–3436.

Received January 26, 2005; returned for revision February 16, 2005; accepted February 17, 2005.


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