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Glycobiology Advance Access published online on July 11, 2008
Glycobiology, doi:10.1093/glycob/cwn061
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Review

Strategies for Carbohydrate Recognition by the Mannose 6-Phosphate Receptors

Nancy M. Dahms1, Linda J. Olson and Jung-Ja P. Kim1

Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

1 To whom correspondence should be addressed: Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226. Nancy M. Dahms, phone: (414) 456-4698, fax: (414) 456-6510, email: ndahms{at}mcw.edu Jung-Ja P. Kim, phone: (414) 955-8479, fax: (414) 456-6510, email: jjkim{at}mcw.edu

Received on April 17, 2008; accepted on June 19, 2008

The two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best characterized function of the MPRs is their ability to direct the delivery of ~60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues.

Key words: lectin / lysosome / mannose 6-phosphate receptor / protein targeting


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