doi: 10.1016/j.exer.2012.02.014. Epub 2012 Mar 1.
Focus on molecules: sulfotyrosine
Affiliations
- PMID:22406006
- PMCID: PMC3629733
- DOI: 10.1016/j.exer.2012.02.014
Item in Clipboard
Focus on molecules: sulfotyrosine
Yogita Kanan et al. Exp Eye Res.2012 Dec.
Display options
Format
Display options
Format
No abstract available
Figures
A. Figure 1. Synthetic pathway for generation of sulfotyrosine and localization of sulfotyrosine proteins in mouse eye. A. The enzymatic generation of sulfotyrosine. Sulfate donor 3'-phosphoadenosine 5'¬phosphosulfate (PAPS) is translocated into the trans-Golgi network (TGN) by the enzyme PAPS translocase from the cytoplasm where it is synthesized. Once inside the TGN, TPST-1/2 located in the TGN membrane incorporates the sulfate residue from PAPS into tyrosine residues of secreted and transmembrane proteins. The sulfotyrosine-containing proteins are then incorporated into vesicles to be transported to their final destination, which may either be the plasma membrane or the extracellular space. B-D. Localization of tyrosine sulfated proteins in ocular tissues. Sections were stained with anti-sulfotyrosine antibody (green) and the cell nuclei were counterstained with DAPI (blue). B. Tyrosine sulfated proteins are present in the cornea (C), and in the zonule fibers (ZF) and their attachments to the ciliary body (CB) and the lens. C. Tyrosine sulfated proteins are abundant in the sclera, choroid, Bruch's membrane (BM), and the connective tissue associated with the extraocular muscles (EOM). The retinal pigmented epithelium (RPE) and skeletal muscle cells of the EOM also show labeling for tyrosine sulfated proteins, but at much lower levels than the surrounding connective tissues. D. Tyrosine sulfated proteins are present in all layers of the retina, but are most abundant in the interphotoreceptor matrix surrounding the photoreceptor outer segments (OS) and at the inner limiting membrane (ILM). IS, inner segments; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars = 100 μm for B; 20 μm for C and D.
Similar articles
- Sulphation of tyrosine residues-a widespread modification of proteins.Huttner WB.Huttner WB.Nature. 1982 Sep 16;299(5880):273-6. doi: 10.1038/299273a0.Nature. 1982.PMID:6180325No abstract available.
- Sulfation of nitrotyrosine: biochemistry and functional implications.Liu MC, Yasuda S, Idell S.Liu MC, et al.IUBMB Life. 2007 Oct;59(10):622-7. doi: 10.1080/15216540701589320.IUBMB Life. 2007.PMID:17891604Review.
- Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands.Moussouras NA, Getschman AE, Lackner ER, Veldkamp CT, Dwinell MB, Volkman BF.Moussouras NA, et al.Int J Mol Sci. 2017 Sep 3;18(9):1894. doi: 10.3390/ijms18091894.Int J Mol Sci. 2017.PMID:28869519Free PMC article.
- Molecular recognition of sulfotyrosine and phosphotyrosine by the Src homology 2 domain.Ju T, Niu W, Cerny R, Bollman J, Roy A, Guo J.Ju T, et al.Mol Biosyst. 2013 Jul;9(7):1829-32. doi: 10.1039/c3mb70061e. Epub 2013 Apr 9.Mol Biosyst. 2013.PMID:23567872
- Tyrosine sulfation: a modulator of extracellular protein-protein interactions.Kehoe JW, Bertozzi CR.Kehoe JW, et al.Chem Biol. 2000 Mar;7(3):R57-61. doi: 10.1016/s1074-5521(00)00093-4.Chem Biol. 2000.PMID:10712936Review.
Cited by
- Sulfotransferase activity contributes to long-term potentiation and long-term memory.Sahoo B, Sharma SK.Sahoo B, et al.Learn Mem. 2022 May 19;29(6):155-159. doi: 10.1101/lm.053538.121. Print 2022 Jun.Learn Mem. 2022.PMID:35589338Free PMC article.
- Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.Bashyal A, Brodbelt JS.Bashyal A, et al.Mass Spectrom Rev. 2024 Mar-Apr;43(2):289-326. doi: 10.1002/mas.21811. Epub 2022 Sep 27.Mass Spectrom Rev. 2024.PMID:36165040Free PMC article.Review.
- Characterization, Dynamics, and Mechanism of CXCR4 Antagonists on a Constitutively Active Mutant.Rosenberg EM Jr, Harrison RES, Tsou LK, Drucker N, Humphries B, Rajasekaran D, Luker KE, Wu CH, Song JS, Wang CJ, Murphy JW, Cheng YC, Shia KS, Luker GD, Morikis D, Lolis EJ.Rosenberg EM Jr, et al.Cell Chem Biol. 2019 May 16;26(5):662-673.e7. doi: 10.1016/j.chembiol.2019.01.012. Epub 2019 Feb 28.Cell Chem Biol. 2019.PMID:30827936Free PMC article.
References
- Higuchi M, Wong C, Kochhan L, Olek K, Aronis S, Kasper CK, Kazazian HH, Jr., Antonarakis SE. Characterization of mutations in the factor VIII gene by direct sequencing of amplified genomic DNA. Genomics. 1990;6:65–71. - PubMed
- Kanan Y, Hamilton RA, Moore KL, Al-Ubaidi MR. Protein tyrosine-o-sulfation in bovine ocular tissues. Adv.Exp.Med.Biol. 2012;723:835–841. - PubMed
- Moore KL. The biology and enzymology of protein tyrosine O-sulfation. J.Biol.Chem. 2003;278:24243–24246. - PubMed
MeSH terms
Substances
Related information
Grants and funding
LinkOut - more resources
Full Text Sources