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A more recent version of this article appeared on April 27, 2007
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M701588200v1
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Papers In Press, published online ahead of print February 23, 2007
J. Biol. Chem, 10.1074/jbc.M701588200
Submitted on February 22, 2007
Accepted on February 23, 2007

Disruption of the GDNF binding site in NCAM dissociates ligand binding and homophilic cell adhesion

Dan Sjöstrand, Jonas Carlsson, Gustavo Paratcha, Bengt Persson, and Carlos F. Ibáñez

Dept. of Neuroscience, Karolinska Institute, Stockholm 17177

Corresponding Author: carlos.ibanez{at}ki.se

Most plasma membrane proteins are capable of sensing multiple cell-cell and cell-ligand interactions, but the extent to which this functional versatility is founded on their modular design is less clear. We have identified the third Ig domain of the Neural Cell Adhesion Molecule NCAM as the necessary and sufficient determinant for its interaction with Glial Cell Line-Derived Neurotrophic Factor (GDNF). Four charged contacts were identified by molecular modeling as the main contributors to binding energy. Their mutation abolished GDNF binding to NCAM, but left intact NCAM’s ability to mediate cell adhesion, indicating that the two functions are genetically separable. The GDNF-NCAM interface allows complex formation with the GFRa1 co-receptor, shedding light on the molecular architecture of a multi-component GDNF receptor.


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D. Sjostrand and C. F. Ibanez
Insights into GFR{alpha}1 Regulation of Neural Cell Adhesion Molecule (NCAM) Function from Structure-Function Analysis of the NCAM/GFR{alpha}1 Receptor Complex
J. Biol. Chem., May 16, 2008; 283(20): 13792 - 13798.
[Abstract] [Full Text] [PDF]


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