It takes two—or more—to tango: Revisiting the role of dopamine transporter oligomerization
Autor: | Harald H. Sitte, Ulrik Gether |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
monoamine transporters Allosteric regulation AL AIM-100-like compound Endocytosis Biochemistry Reuptake oligomerization 03 medical and health sciences Editors' Pick Highlight Dopamine DAT dopamine transporter medicine Animals Humans endocytosis Neurotransmitter sodium symporter Molecular Biology dopamine transporter Dopamine transporter Dopamine Plasma Membrane Transport Proteins dimerization allosteric modulation 030102 biochemistry & molecular biology biology Chemistry Transporter Cell Biology SERT serotonin Transmembrane protein 030104 developmental biology NET norepinephrine biology.protein Biophysics NSS neurotransmitter:sodium symporter Protein Multimerization medicine.drug TM transmembrane |
Zdroj: | The Journal of Biological Chemistry Gether, U & Sitte, H H 2021, ' It takes two-or more-to tango : Revisiting the role of dopamine transporter oligomerization ', Journal of Biological Chemistry, vol. 296, 100629 . https://doi.org/10.1016/j.jbc.2021.100629 |
ISSN: | 1083-351X 0021-9258 |
DOI: | 10.1016/j.jbc.2021.100629 |
Popis: | The dopamine transporter utilizes the transmembrane sodium gradient to mediate reuptake of dopamine from the extracellular space. The dopamine transporter can form dimers and possibly also higher order structures in the plasma membrane, and this oligomerization has been implicated in both trafficking and transport. However, we still do not fully understand its biological importance. A study by Sorkina et al. now describes a series of small molecules that link transporter conformation to oligomerization and endocytosis, providing an interesting step forward in an intricate dance. |
Databáze: | OpenAIRE |
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