Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export

Nufer, O. and Guldbrandsen, S. and Degen, M. and Kappeler, F. and Paccaud, J. -P. and Tani, K. and Hauri, H. -P.. (2002) Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export. Journal of cell science, Vol. 115, H. 3. pp. 619-628.

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Official URL: http://edoc.unibas.ch/dok/A5257760

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Export of membrane proteins from the ER is believed to be selective and require transport signals, but the identity of such signals has remained elusive. The recycling type I membrane protein ERGIC-53 carries a C-terminal diphenylalanine motif that is required for efficient ER export. Here we show that this motif can be functionally substituted by a single phenylalanine or tyrosine at position -2, two leucines or isoleucines at position -1 and -2 or a single valine at position -1. These motifs are common among mammalian type I membrane proteins. A single C-terminal valine, but none of the other motifs, accelerates transport of inefficiently exported reporter constructs and hence operates as an export signal. The valine signal is position, but not context, dependent. All transport motifs mediate COPII binding in vitro with distinct preferences for the COPII subunits Sec23p, Sec24Bp, Sec24Cp and p125. These results suggest that cytoplasmic C-terminal amino-acid motifs, either alone or in conjunction with other transport determinants, accelerate ER export of numerous type I and probably polytopic membrane proteins by mediating interaction with COPII coat components.
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
Publisher:Company of Biologists
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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