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Vol. 16, Issue 3, 1258-1267, March 2005
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* Department of Pharmacology and Neurobiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
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 
-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/-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.
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.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
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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