N-linked oligosaccharides on the low density lipoprotein receptor homolog SorLA/LR11 are modified with terminal GalNAc-4-SO4 in kidney and brain

Dorothy Fiete, Yiling Mi, Edward L. Oats, Mary C. Beranek, Jacques U. Baenziger

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

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 β1,4-linked GalNAc-4-SO4. Oligosaccharides located in the vacuolar sorting (Vps) 10p domain (Vps10p domain) are modified with β1,4-linked GalNAc when the Vps10p domain is expressed in cells along with either of two recently cloned protein-specific β1,4GalNAc-transferases, GalNAcTIII and GalNAcTIV. Either of two sequences with basic amino acids located within the Vps10p domain is able to mediate recognition by these β1,4GalNAc-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.

Original languageEnglish
Pages (from-to)1873-1881
Number of pages9
JournalJournal of Biological Chemistry
Volume282
Issue number3
DOIs
StatePublished - Jan 19 2007

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