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  Heterologously Expressed GLT-1 Associates in ~200-nm Protein-Lipid Islands

Raunser, S., Haase, W., Franke, C., Eckert, G., Müller, W. E., & Kühlbrandt, W. (2006). Heterologously Expressed GLT-1 Associates in ~200-nm Protein-Lipid Islands. Biophysical Journal (Annual Meeting Abstracts), 91, 3718-3726. doi:10.1529/biophysj.106.086900.

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 Creators:
Raunser, Stefan1, Author           
Haase, Winfried1, Author           
Franke, Cornelia2, Author
Eckert, Gunter2, Author
Müller, Walter E.2, Author
Kühlbrandt, Werner1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Department of Pharmacology, Biocenter Niederursel, University of Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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 Abstract: The glutamate transporter GLT-1 from Rattus norvegicus was expressed at high level in baby hamster kidney (BHK-21) cells by the Semliki Forest Virus expression system. We examined the expressed GLT-1 in the plasma membrane and found that the transporter accumulates in detergent-insoluble lipid-protein assemblies. Freeze-fracture, immunogold labeling, and electron microscopy revealed that GLT-1 forms approximately 200-nm protein-rich islands in the plasma membrane. Cholesterol depletion in living cells resulted in a dispersion of the GLT-1 islands, indicating that they are the result of lipid-protein rather than protein-protein interactions. Disruption of GLT-1 islands and dispersion of GLT-1 goes along with a reduction of the glutamate transport activity. Our direct visualization of lipid-protein islands in the plasma membrane of tissue culture cells suggests that the reported clustering of glutamate transporters and their cholesterol-dependent transport activity in cells is likewise connected to their association with cholesterol-rich microdomains in the plasma membrane.

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Language(s): eng - English
 Dates: 2006
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 305054
DOI: 10.1529/biophysj.106.086900
 Degree: -

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Title: Biophysical Journal (Annual Meeting Abstracts)
  Other : Biophys. J. (Annual Meeting Abstracts)
Source Genre: Journal
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Publ. Info: Bethesda, MD : Biophysical Society
Pages: - Volume / Issue: 91 Sequence Number: - Start / End Page: 3718 - 3726 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117_1