HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 3, 1873-1881, January 19, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/3/1873    most recent M606455200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fiete, D. Articles by Baenziger, J. U. Search for Related Content PubMed PubMed Citation Articles by Fiete, D. Articles by Baenziger, J. U. Social Bookmarking                      What's this?

N-Linked Oligosaccharides on the Low Density Lipoprotein Receptor Homolog SorLA/LR11 Are Modified with Terminal GalNAc-4-SO₄ in Kidney and Brain^*

From the Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110

Sorting protein-related receptor (SorLA/LR11) is a highly conserved mosaic receptor that is expressed by cells in a number of different tissues including principal cells of the collecting ducts in the kidney and neurons in the central and peripheral nervous systems. SorLA/LR11 has features that indicate it serves as a sorting receptor shuttling between the plasma membrane, endosomes, and the Golgi. We have found that a fraction of SorLA/LR11 that is synthesized in the kidney and the brain bears N-linked oligosaccharides that are modified with terminal 1,4-linked GalNAc-4-SO₄. Oligosaccharides located in the vacuolar sorting (Vps) 10p domain (Vps10p domain) are modified with 1,4-linked GalNAc when the Vps10p domain is expressed in cells along with either of two recently cloned protein-specific 1,4GalNAc-transferases, GalNAcTIII and GalNAcTIV. Either of two sequences with basic amino acids located within the Vps10p domain is able to mediate recognition by these 1,4GalNAc-transferases. The highly specific modification of oligosaccharides in the Vps10p domain of SorLA/LR11 with terminal GalNAc-4-SO₄ suggests that this unusual modification may modulate the interaction of SorLA/LR11 with proteins and influence their trafficking.

Received for publication, July 6, 2006 , and in revised form, November 14, 2006.

^* This work was supported by the National Institutes of Health Grants R01-DK41738 and R37-CA21923. 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.

¹ To whom correspondence should be addressed: 4940 Parkview Place, St. Louis, MO 63110. Tel.: 314-362-8730; Fax: 314-362-8888; E-mail: Baenziger{at}Pathology.wustl.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. Miller, D. Fiete, N. M. J. Blake, M. Beranek, E. L. Oates, Y. Mi, D. S. Roseman, and J. U. Baenziger A Necessary and Sufficient Determinant for Protein-selective Glycosylation in Vivo J. Biol. Chem., January 25, 2008; 283(4): 1985 - 1991. [Abstract] [Full Text] [PDF]