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Originally published In Press as doi:10.1074/jbc.M511872200 on March 10, 2006

J. Biol. Chem., Vol. 281, Issue 18, 12986-12993, May 5, 2006
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The MRH Protein Erlectin Is a Member of the Endoplasmic Reticulum Synexpression Group and Functions in N-Glycan Recognition*Formula

Cristina-Maria Cruciat1, Christine Hassler12, and Christof Niehrs3

From the Department of Molecular Embryology, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany

Kremen1 and 2 (Krm1/2) are coreceptors for Dickkopf1 (Dkk1), an antagonist of Wnt/beta-catenin signaling, and play a role in head induction during early Xenopus development. In a proteomic approach we identified Erlectin, a novel protein that interacts with Krm2. Erlectin (XTP3-B) is member of a protein family containing mannose 6-phosphate receptor homology (MRH-, or PRKCSH-) domains implicated in N-glycan binding. Like other members of the MRH family, Erlectin is a luminal resident protein of the endoplasmic reticulum. It contains two MRH domains, of which one is essential for Krm2 binding, and this interaction is abolished by Krm2 deglycosylation. The overexpression of Erlectin inhibits transport of Krm2 to the cell surface. Analysis of its embryonic expression pattern in Xenopus reveals that Erlectin is member of the endoplasmic reticulum synexpression group. Erlectin morpholino antisense injection leads to head and axial defects during organogenesis stages in Xenopus embryos. The results indicate that Erlectin functions in N-glycan recognition in the endoplasmic reticulum, suggesting that it may regulate glycoprotein traffic.


Received for publication, November 3, 2005 , and in revised form, March 9, 2006.

* This work was supported in part by the European Union grant (Endotrack). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental Table 1 and Fig. 1.

1 Both authors contributed equally to this work.

2 Supported by a DFG fellowship (GRK 791).

3 To whom correspondence should be addressed. E-mail: niehrs{at}dkfz-heidelberg.de.


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