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First published online September 26, 2003

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ER export – a complete picture

Export of proteins from the ER appears to involve default pathways (bulk flow) and selective mechanisms. Selective export depends on sorting signals in the protein – for example, FF, di-acidic and di-hydrophobic motifs. These have not been fully characterized and, in most cases, efficient export seems to require several regions of the protein. Hans-Peter Hauri and co-workers now provide the first complete map of export determinants for a type I membrane protein: ERGIC-53, a protein that cycles between the ER and the ER-Golgi intermediate compartment (ERGIC). Using endoglycosidase resistance to monitor export of ERGIC-53 mutants biochemically, they identify determinants in the cytoplasmic, lumenal and transmembrane regions of ERGIC-53 (see p. 4429). These include the F2 residue at the C-terminus (which interacts with the vesicle coat protein COPII), transmembrane residues that facilitate oligomerization and lumenal cysteine residues necessary for disulphide-mediated stabilization of ERGIC-53 oligomers. Importantly, the authors show that when these determinants are placed on a signal-less reporter protein it is efficiently exported. They conclude that the transmembrane and lumenal motifs cooperate to promote ERGIC-53 oligomerization, which is essential for efficient recruitment of the protein's C-terminus by the COPII export machinery.

Related articles in JCS:

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

Oliver Nufer, Felix Kappeler, Svend Guldbrandsen, and Hans-Peter Hauri
JCS 2003 116: 4429-4440. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content