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Signals and mechanisms for protein retention in the endoplasmic reticulum

Sophie Pagny, Patrice Lerouge, Loïc Faye and Véronique Gomord
Journal of Experimental Botany
Vol. 50, No. 331 (FEBRUARY 1999), pp. 157-164
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/23695674
Page Count: 8
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Signals and mechanisms for protein retention in the endoplasmic reticulum
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Abstract

After their co-translational insertion into the ER lumen or the ER membrane, most proteins are transported via the Golgi apparatus downstream on the secretory pathway while a few protein species are retained in the ER. Polypeptide retention in the ER is either signal-independent or depends on specific retention signals encoded by the primary sequence of the polypeptide. A first category, i.e. the newly synthesized polypeptides that are unable to reach their final conformation, are retained in the ER where this quality control generally results in their degradation. A second category, namely the ER-resident proteins escape the bulk flow of secretion due to the presence of a specific N- or C-terminal signal that interacts with integral membrane or soluble receptors. ER retention of soluble proteins mediated by either KDEL, HDEL or related sequences and membrane receptors has been relatively well characterized in plants. Recent efforts have aimed at a characterization of the retention signal(s) of type I membrane proteins in the plant ER.

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