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Papers In Press, published online ahead of print January 17, 2002
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226
Corresponding Author: ndahms{at}mcw.edu
Two distinct mannose 6-phosphate (M6P) receptors (MPRs), the cation-dependent MPR (CD-MPR) and the insulin-like growth factor II/MPR (IGF-II/MPR), recognize a diverse population of M6P-containing ligands. The IGF-II/MPR is a type I transmembrane glycoprotein with a large extracytoplasmic region comprised of 15 repeating domains that display sequence identity to each other and to the single extracytoplasmic domain of the CD-MPR. A structure-based sequence alignment of the two distinct M6P binding sites of the IGF-II/MPR with the CD-MPR implicates several residues of IGF-II/MPR domains 3 and 9 as essential for M6P binding. To test this hypothesis single amino acid substitutions were made in constructs encoding either the N- or the C-terminal M6P binding sites of the bovine IGF-II/MPR. The mutant IGF-II/MPRs secreted from COS-1 cells were analyzed by pentamannosyl phosphate-agarose affinity chromatography, identifying four residues (Q392, S431, E460, and Y465) in domain 3 and four residues (Q1292, H1329, E1354, and Y1360) in domain 9 as essential for M6P recognition. Binding affinity studies using the lysosomal enzyme,
J. Biol. Chem, 10.1074/jbc.M109855200
Submitted on October 11, 2001
Revised on December 31, 2001
Accepted on January 16, 2002
Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor
-glucuronidase, confirmed these results. Together these analyses provide strong evidence that the two M6P binding sites of the IGF-II/MPR are structurally similar to each other and to the CD-MPR and utilize a similar carbohydrate recognition mechanism.
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