Post-translational modifications of serotonin transporter
| Autor: | Fusun Kilic, Donna S. Woulfe, Anthonya Cooper |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Glycosylation Serotonylation 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Diabetes Mellitus Animals Humans Phosphorylation Serotonin transporter Serotonin Plasma Membrane Transport Proteins Pharmacology chemistry.chemical_classification biology Transporter Sialic acid Cell biology Insulin receptor 030104 developmental biology chemistry 030220 oncology & carcinogenesis biology.protein Serotonin Glycoprotein Protein Processing Post-Translational |
| Zdroj: | Pharmacological Research. 140:7-13 |
| ISSN: | 1043-6618 |
| DOI: | 10.1016/j.phrs.2018.10.018 |
| Popis: | The serotonin transporter (SERT) is an oligomeric glycoprotein with two sialic acid residues on each of two complex oligosaccharide molecules. Studies using in vivo and in vitro model systems demonstrated that diverse post-translational modifications, including phosphorylation, glycosylation, serotonylation, and disulfide bond formation, all favorably influences SERT conformation and allows the transporter to function most efficiently. This review discusses the post-translational modifications and their importance on the structure, maturation, and serotonin (5-HT) uptake ability of SERT. Finally, we discuss how these modifications are altered in diabetes mellitus and subsequently impairs the 5-HT uptake ability of SERT. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect