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Updated: Jul 4, 2026

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
Published on: November 27, 2016
Membrane glycoprotein M6B interacts with the human serotonin transporter
Anja Winther Fjorback1, Heidi Kaastrup Müller, Ove Wiborg
1Centre for Psychiatric Research, University Hospital of Aarhus, Risskov, Denmark.
The membrane glycoprotein M6B binds to the serotonin transporter (SERT), reducing serotonin uptake by decreasing SERT
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- The serotonin transporter (SERT) regulates serotonin levels in the synapse.
- The function of the M6B proteolipid protein family in the brain is not well understood.
- M6B is hypothesized to be involved in cellular housekeeping functions.
Purpose of the Study:
- To identify binding partners of the serotonin transporter (SERT).
- To investigate the functional interaction between SERT and its binding partners.
- To elucidate the role of M6B in regulating serotonin transporter activity.
Main Methods:
- Yeast two-hybrid system for identifying protein interactions.
- Co-immunoprecipitation and glutathione-S-transferase pull-down assays for interaction verification.
- Confocal microscopy to assess protein co-localization and surface expression.
Main Results:
- The membrane glycoprotein M6B was identified as a SERT binding partner.
- Co-expression of M6B with SERT significantly decreased serotonin uptake.
- M6B co-localizes with SERT in cellular models and endogenous cells, indicating a regulatory complex.
Conclusions:
- M6B directly interacts with SERT.
- M6B binding leads to reduced SERT-mediated serotonin uptake.
- M6B regulates serotonin transporter function, likely through modulation of its cellular trafficking and surface expression.
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