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ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains

Nufer, O. and Kappeler, F. and Guldbrandsen, S. and Hauri, H. -P.. (2003) ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains. Journal of cell science, Vol. 116, H. 21. pp. 4429-4440.

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Official URL: http://edoc.unibas.ch/dok/A5257755

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Abstract

Selective export of proteins from the endoplasmic reticulum (ER) requires transport signals that have not been fully characterized. Here, we provide the first complete map of ER export determinants of a type I membrane protein, ERGIC-53, that cycles in the early secretory pathway. ER export requires a phenylalanine motif at the C-terminus, known to mediate coat protein II (COPII) interaction, that is assisted by a glutamine in the cytoplasmic domain. Disulfide bond-stabilized oligomerization is also required. Efficient hexamerization depends on the presence of a polar and two aromatic residues in the transmembrane domain (TMD). Oligomerization becomes independent on disulfide bonds when TMD hydrophobicity is increased. ER export is also influenced by TMD length, 21 amino acids being most efficient. When transferred to a signal-less construct, the established targeting motifs reconstitute full transport activity. The results suggest an ER-export mechanism in which transmembrane and luminal determinants mediate oligomerization required for efficient recruitment of ERGIC-53 into budding vesicles via the C-terminal COPII-binding phenylalanine motif.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri)
UniBasel Contributors:Hauri, Hans-Peter
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Company of Biologists
ISSN:0021-9533
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:18

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