Rer1, a putative transmembrane domain receptor responsible for targeting proteins to the endoplasmic reticulum |
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Authors: | Joachim Füllekrug |
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Affiliation: | (1) Cell Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany;(2) Heidelberg and Max-Planck-Institute for Molecular Cell Biology and Genetics, Dresden |
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Abstract: | Summary Localization of resident proteins provides identity to subcellular compartments. Most proteins depend on a combination of both retention and retrieval to maintain their steady-state distribution. Rerl is a putative receptor protein mediating retrieval of membrane proteins of the endoplasmic reticulum. This retrieval relies on an unusual hydrophobic target sequence, the transmembrane domain. Apart from Rerl, coatomer is also required to retrieve escaped membrane proteins from the early Golgi region back to the endoplasmic reticulum. Current evidence suggests that the Rerl-mediated retrieval of membrane proteins is a general sorting pathway in eukaryotic cells contributing to the maintenance of compartmental identity in the early secretory pathway. |
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Keywords: | Rer1 Transmembrane domain Endoplasmic-reticulum localization Sec12p |
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