Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print January 5, 2005
Mol. Biol. Cell 10.1091/mbc.E04-08-0708

A more recent version of this article appeared on March 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E04-08-0708v1
16/3/1258    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Appenzeller-Herzog, C.
Right arrow Articles by Hauri, H.-P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Appenzeller-Herzog, C.
Right arrow Articles by Hauri, H.-P.

Submitted on August 17, 2004
Revised on November 22, 2004
Accepted on December 16, 2004

Carbohydrate- and Conformation-dependent Cargo Capture for ER-Exit

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

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

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.

Present addresses: {dagger}Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland; ||Bone and Mineral Research Unit, Hospital Universitario Central de Asturias, 33006 Oviedo, Spain.

Corresponding author. E-mail: Hans-Peter.Hauri{at}unibas.ch






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.