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Membrane Cholesterol Modulates Serotonin Transporter Activity

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 2001, 40, 35, 10507-10513
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    Membrane Cholesterol Modulates Serotonin Transporter Activity†
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    Biochemistry Department, Trinity College, Dublin 2, Ireland, and Biochemical Laboratory, Central Institute for Mental Health, 68159 Mannheim, Germany
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    Biochemistry

    Cite this: Biochemistry 2001, 40, 35, 10507–10513
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    https://doi.org/10.1021/bi010730z
    Published August 10, 2001
    Copyright © 2001 American Chemical Society
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    Abstract

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    The synaptic actions of the neurotransmitter serotonin are terminated by a selective high-affinity reuptake mediated by the serotonin transporter (SERT). To gain insight into the modulation of the functional properties of this integral membrane protein by cholesterol, a main component of the lipid bilayer, we stably expressed the rat SERT in human embryonic kidney 293 cells and, upon altering the cholesterol content of these cells by different means, analyzed SERT activity. Depletion of the level of membrane cholesterol by treatment with either the cholesterol chelating agent methyl-β-cyclodextrin (MβCD), cholesterol oxidase, or the cholesterol-binding fluorochrome filipin resulted in a decrease in SERT activity due to both a loss of affinity of substrate and ligand binding and a concomitant reduction of the maximal transport rate. In cholesterol-depleted membranes, cholesterol levels could be restored to those found in untreated membranes by incubation of the membranes with an MβCD−cholesterol complex, which correlated with a reversal of the cholesterol depletion-mediated decrease in the level of high-affinity binding. This was not the case when other steroids, such as ergosterol, 5-cholestene, or pregnenolone, were substituted into cholesterol-depleted membranes. These results suggest that membrane cholesterol modulates the functional properties of the SERT by specific molecular interactions which are needed to stabilize the transporter in its optimally active form.

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    †

     This work was supported by the Deutsche Forschungsgemeinschaft (SCHL 353/4-1 to P.S.), EU TMR Contract CT98−0277 to D.C.W., and a BioResearch Ireland training studentship to S.M.S.

    ‡

     Trinity College.

    §

     Central Institute for Mental Health.

    *

     To whom correspondence should be addressed. Telephone:  +0049-621-1703-835. Fax:  +0049-621-1703-837. E-mail:  [email protected].

    Cited By

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    This article is cited by 151 publications.

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    Biochemistry

    Cite this: Biochemistry 2001, 40, 35, 10507–10513
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    https://doi.org/10.1021/bi010730z
    Published August 10, 2001
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