O -Linked Glycosylation at Threonine 27 Protects the Copper Transporter hCTR1 from Proteolytic Cleavage in Mammalian Cells *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 282, Issue: 28, Page: 20376-20387
2007
- 72Citations
- 62Captures
- 1Mentions
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Metrics Details
- Citations72
- Citation Indexes72
- 72
- CrossRef54
- Captures62
- Readers62
- 62
- Mentions1
- References1
- Wikipedia1
Article Description
The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa. hCTR1 antibodies recognize multiple bands in SDS-PAGE centered at 35 kDa. Part of this increased mass is due to N -linked glycosylation at Asn-15. We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1. We demonstrate that the extracellular amino terminus of hCTR1 also contains O- linked polysaccharides. Glycosidase treatment that removed O- linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1–2 kDa. Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O- linked glycosylation to Thr-27. Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations. This cleavage produced a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1. Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O- glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide. The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1. Thus, O- linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819780302; http://dx.doi.org/10.1074/jbc.m701806200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=34547131326&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17525160; https://linkinghub.elsevier.com/retrieve/pii/S0021925819780302; http://www.jbc.org/lookup/doi/10.1074/jbc.M701806200; https://syndication.highwire.org/content/doi/10.1074/jbc.M701806200; https://dx.doi.org/10.1074/jbc.m701806200
Elsevier BV
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