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Originally published as MBC in Press, 10.1091/mbc.E04-08-0708 on January 5, 2005

Vol. 16, Issue 3, 1258-1267, March 2005

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Carbohydrate- and Conformation-dependent Cargo Capture for ER-Exit{boxd}

Christian Appenzeller-Herzog * {dagger}, Beat Nyfeler *, Peter Burkhard {ddagger}, Inigo Santamaria § ||, Carlos Lopez-Otin §, and Hans-Peter Hauri *

* Department of Pharmacology and Neurobiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; {ddagger} M. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; and § Departamento de Bioquimica y Biologia Molecular, Instituto Universitario de Oncologia, Universidad de Oviedo, 33006-Oviedo, Spain

Submitted August 17, 2004; Revised November 22, 2004; Accepted December 16, 2004
Monitoring Editor: Reid Gilmore

Some secretory proteins leave the endoplasmic reticulum (ER) by a receptor-mediated cargo capture mechanism, but the signals required for the cargo-receptor interaction are largely unknown. Here, we describe a novel targeting motif that is composed of a high-mannose type oligosaccharide intimately associated with a surface-exposed peptide {beta}-hairpin loop. The motif accounts for lectin ERGIC-53–assisted ER-export of the lyososomal enzyme procathepsin Z. The second oligosaccharide chain of procathepsin Z exhibits no binding activity for ERGIC-53, illustrating the selective lectin properties of ERGIC-53. Our data suggest that the conformation-based motif is only present in fully folded procathepsin Z and that its recognition by ERGIC-53 reflects a quality control mechanism that acts complementary to the primary folding machinery in the ER. A similar oligosaccharide/{beta}-hairpin loop structure is present in cathepsin C, another cargo of ERGIC-53, suggesting the general nature of this ER-exit signal. To our knowledge this is the first documentation of an ER-exit signal in soluble cargo in conjunction with its decoding by a transport receptor.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-08-0708) on January 5, 2005.

Abbreviations used: catZ, cathepsin Z; catZr, cathepsin Z–related protein; DSP, dithiobis(succinimidylpropionate); endoH, endoglycosidase H; ER, endoplasmic reticulum; procatZ, procathepsin Z; wt, wild-type.

{boxd} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

{dagger} Present address: Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland

|| Present address: Bone and Mineral Research Unit, Hospital Universitario Central de Asturias, 33006 Oviedo, Spain

Address correspondence to: Hans-Peter Hauri (Hans-Peter.Hauri{at}unibas.ch).




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