Skip Navigation


Glycobiology Advance Access originally published online on July 11, 2008
Glycobiology 2008 18(9):664-678; doi:10.1093/glycob/cwn061
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
18/9/664    most recent
cwn061v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Dahms, N. M
Right arrow Articles by Kim, J.-J. P
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dahms, N. M
Right arrow Articles by Kim, J.-J. P
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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, WI 53226, USA

1 To whom correspondence should be addressed: Tel: +1-414-456-4698; Fax: +1-414-456-6510; e-mail: ndahms{at}mcw.edu and jjkim{at}mcw.edu

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
M. Boonen, P. Vogel, K. A. Platt, N. Dahms, and S. Kornfeld
Mice Lacking Mannose 6-Phosphate Uncovering Enzyme Activity Have a Milder Phenotype than Mice Deficient for N-Acetylglucosamine-1-Phosphotransferase Activity
Mol. Biol. Cell, October 15, 2009; 20(20): 4381 - 4389.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.