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Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae
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| Zeitschriftentitel: | Eukaryotic Cell |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Eukaryotic Cell, 5, 2006, 6, S. 945-953 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar |
|---|---|
| author |
Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar |
| spellingShingle |
Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar Eukaryotic Cell Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae Molecular Biology General Medicine Microbiology |
| author_sort |
grossmann, guido |
| spelling |
Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar 1535-9778 1535-9786 American Society for Microbiology Molecular Biology General Medicine Microbiology http://dx.doi.org/10.1128/ec.00206-05 <jats:title>ABSTRACT</jats:title> <jats:p> The hexose-proton symporter HUP1 shows a spotty distribution in the plasma membrane of the green alga <jats:italic>Chlorella kessleri. Chlorella</jats:italic> cannot be transformed so far. To study the membrane localization of the HUP1 protein in detail, the symporter was fused to green fluorescent protein (GFP) and heterologously expressed in <jats:italic>Saccharomyces cerevisiae</jats:italic> and <jats:italic>Schizosaccharomyces pombe</jats:italic> . In these organisms, the HUP1 protein has previously been shown to be fully active. The GFP fusion protein was exclusively targeted to the plasma membranes of both types of fungal cells. In <jats:italic>S. cerevisiae</jats:italic> , it was distributed nonhomogenously and concentrated in spots resembling the patchy appearance observed previously for endogenous H <jats:sup>+</jats:sup> symporters. It is documented that the <jats:italic>Chlorella</jats:italic> protein colocalizes with yeast proteins that are concentrated in 300-nm raft-based membrane compartments. On the other hand, it is completely excluded from the raft compartment housing the yeast H <jats:sup>+</jats:sup> /ATPase. As judged by their solubilities in Triton X-100, the HUP1 protein extracted from <jats:italic>Chlorella</jats:italic> and the GFP fusion protein extracted from <jats:italic>S. cerevisiae</jats:italic> are detergent-resistant raft proteins. <jats:italic>S. cerevisiae</jats:italic> mutants lacking the typical raft lipids ergosterol and sphingolipids showed a homogenous distribution of HUP1-GFP within the plasma membrane. In an ergosterol synthesis ( <jats:italic>erg6</jats:italic> ) mutant, the rate of glucose uptake was reduced to less than one-third that of corresponding wild-type cells. In <jats:italic>S. pombe</jats:italic> , the sterol-rich plasma membrane domains can be stained in vivo with filipin. <jats:italic>Chlorella</jats:italic> HUP1-GFP accumulated exactly in these domains. Altogether, it is demonstrated here that a plant membrane protein has the property of being concentrated in specific raft-based membrane compartments and that the information for its raft association is retained between even distantly related organisms. </jats:p> Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in <i>Saccharomyces cerevisiae</i> Eukaryotic Cell |
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American Society for Microbiology, 2006 |
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2006 |
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American Society for Microbiology |
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Eukaryotic Cell |
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| title |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_unstemmed |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_full |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_fullStr |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_full_unstemmed |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_short |
Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_sort |
lipid raft-based membrane compartmentation of a plant transport protein expressed in
<i>saccharomyces cerevisiae</i> |
| topic |
Molecular Biology General Medicine Microbiology |
| url |
http://dx.doi.org/10.1128/ec.00206-05 |
| publishDate |
2006 |
| physical |
945-953 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
The hexose-proton symporter HUP1 shows a spotty distribution in the plasma membrane of the green alga
<jats:italic>Chlorella kessleri. Chlorella</jats:italic>
cannot be transformed so far. To study the membrane localization of the HUP1 protein in detail, the symporter was fused to green fluorescent protein (GFP) and heterologously expressed in
<jats:italic>Saccharomyces cerevisiae</jats:italic>
and
<jats:italic>Schizosaccharomyces pombe</jats:italic>
. In these organisms, the HUP1 protein has previously been shown to be fully active. The GFP fusion protein was exclusively targeted to the plasma membranes of both types of fungal cells. In
<jats:italic>S. cerevisiae</jats:italic>
, it was distributed nonhomogenously and concentrated in spots resembling the patchy appearance observed previously for endogenous H
<jats:sup>+</jats:sup>
symporters. It is documented that the
<jats:italic>Chlorella</jats:italic>
protein colocalizes with yeast proteins that are concentrated in 300-nm raft-based membrane compartments. On the other hand, it is completely excluded from the raft compartment housing the yeast H
<jats:sup>+</jats:sup>
/ATPase. As judged by their solubilities in Triton X-100, the HUP1 protein extracted from
<jats:italic>Chlorella</jats:italic>
and the GFP fusion protein extracted from
<jats:italic>S. cerevisiae</jats:italic>
are detergent-resistant raft proteins.
<jats:italic>S. cerevisiae</jats:italic>
mutants lacking the typical raft lipids ergosterol and sphingolipids showed a homogenous distribution of HUP1-GFP within the plasma membrane. In an ergosterol synthesis (
<jats:italic>erg6</jats:italic>
) mutant, the rate of glucose uptake was reduced to less than one-third that of corresponding wild-type cells. In
<jats:italic>S. pombe</jats:italic>
, the sterol-rich plasma membrane domains can be stained in vivo with filipin.
<jats:italic>Chlorella</jats:italic>
HUP1-GFP accumulated exactly in these domains. Altogether, it is demonstrated here that a plant membrane protein has the property of being concentrated in specific raft-based membrane compartments and that the information for its raft association is retained between even distantly related organisms.
</jats:p> |
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| author | Grossmann, Guido, Opekarova, Miroslava, Novakova, Linda, Stolz, Jürgen, Tanner, Widmar |
| author_facet | Grossmann, Guido, Opekarova, Miroslava, Novakova, Linda, Stolz, Jürgen, Tanner, Widmar, Grossmann, Guido, Opekarova, Miroslava, Novakova, Linda, Stolz, Jürgen, Tanner, Widmar |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> The hexose-proton symporter HUP1 shows a spotty distribution in the plasma membrane of the green alga <jats:italic>Chlorella kessleri. Chlorella</jats:italic> cannot be transformed so far. To study the membrane localization of the HUP1 protein in detail, the symporter was fused to green fluorescent protein (GFP) and heterologously expressed in <jats:italic>Saccharomyces cerevisiae</jats:italic> and <jats:italic>Schizosaccharomyces pombe</jats:italic> . In these organisms, the HUP1 protein has previously been shown to be fully active. The GFP fusion protein was exclusively targeted to the plasma membranes of both types of fungal cells. In <jats:italic>S. cerevisiae</jats:italic> , it was distributed nonhomogenously and concentrated in spots resembling the patchy appearance observed previously for endogenous H <jats:sup>+</jats:sup> symporters. It is documented that the <jats:italic>Chlorella</jats:italic> protein colocalizes with yeast proteins that are concentrated in 300-nm raft-based membrane compartments. On the other hand, it is completely excluded from the raft compartment housing the yeast H <jats:sup>+</jats:sup> /ATPase. As judged by their solubilities in Triton X-100, the HUP1 protein extracted from <jats:italic>Chlorella</jats:italic> and the GFP fusion protein extracted from <jats:italic>S. cerevisiae</jats:italic> are detergent-resistant raft proteins. <jats:italic>S. cerevisiae</jats:italic> mutants lacking the typical raft lipids ergosterol and sphingolipids showed a homogenous distribution of HUP1-GFP within the plasma membrane. In an ergosterol synthesis ( <jats:italic>erg6</jats:italic> ) mutant, the rate of glucose uptake was reduced to less than one-third that of corresponding wild-type cells. In <jats:italic>S. pombe</jats:italic> , the sterol-rich plasma membrane domains can be stained in vivo with filipin. <jats:italic>Chlorella</jats:italic> HUP1-GFP accumulated exactly in these domains. Altogether, it is demonstrated here that a plant membrane protein has the property of being concentrated in specific raft-based membrane compartments and that the information for its raft association is retained between even distantly related organisms. </jats:p> |
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| spelling | Grossmann, Guido Opekarova, Miroslava Novakova, Linda Stolz, Jürgen Tanner, Widmar 1535-9778 1535-9786 American Society for Microbiology Molecular Biology General Medicine Microbiology http://dx.doi.org/10.1128/ec.00206-05 <jats:title>ABSTRACT</jats:title> <jats:p> The hexose-proton symporter HUP1 shows a spotty distribution in the plasma membrane of the green alga <jats:italic>Chlorella kessleri. Chlorella</jats:italic> cannot be transformed so far. To study the membrane localization of the HUP1 protein in detail, the symporter was fused to green fluorescent protein (GFP) and heterologously expressed in <jats:italic>Saccharomyces cerevisiae</jats:italic> and <jats:italic>Schizosaccharomyces pombe</jats:italic> . In these organisms, the HUP1 protein has previously been shown to be fully active. The GFP fusion protein was exclusively targeted to the plasma membranes of both types of fungal cells. In <jats:italic>S. cerevisiae</jats:italic> , it was distributed nonhomogenously and concentrated in spots resembling the patchy appearance observed previously for endogenous H <jats:sup>+</jats:sup> symporters. It is documented that the <jats:italic>Chlorella</jats:italic> protein colocalizes with yeast proteins that are concentrated in 300-nm raft-based membrane compartments. On the other hand, it is completely excluded from the raft compartment housing the yeast H <jats:sup>+</jats:sup> /ATPase. As judged by their solubilities in Triton X-100, the HUP1 protein extracted from <jats:italic>Chlorella</jats:italic> and the GFP fusion protein extracted from <jats:italic>S. cerevisiae</jats:italic> are detergent-resistant raft proteins. <jats:italic>S. cerevisiae</jats:italic> mutants lacking the typical raft lipids ergosterol and sphingolipids showed a homogenous distribution of HUP1-GFP within the plasma membrane. In an ergosterol synthesis ( <jats:italic>erg6</jats:italic> ) mutant, the rate of glucose uptake was reduced to less than one-third that of corresponding wild-type cells. In <jats:italic>S. pombe</jats:italic> , the sterol-rich plasma membrane domains can be stained in vivo with filipin. <jats:italic>Chlorella</jats:italic> HUP1-GFP accumulated exactly in these domains. Altogether, it is demonstrated here that a plant membrane protein has the property of being concentrated in specific raft-based membrane compartments and that the information for its raft association is retained between even distantly related organisms. </jats:p> Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in <i>Saccharomyces cerevisiae</i> Eukaryotic Cell |
| spellingShingle | Grossmann, Guido, Opekarova, Miroslava, Novakova, Linda, Stolz, Jürgen, Tanner, Widmar, Eukaryotic Cell, Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae, Molecular Biology, General Medicine, Microbiology |
| title | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_full | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_fullStr | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_full_unstemmed | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_short | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| title_sort | lipid raft-based membrane compartmentation of a plant transport protein expressed in <i>saccharomyces cerevisiae</i> |
| title_unstemmed | Lipid Raft-Based Membrane Compartmentation of a Plant Transport Protein Expressed in Saccharomyces cerevisiae |
| topic | Molecular Biology, General Medicine, Microbiology |
| url | http://dx.doi.org/10.1128/ec.00206-05 |