AustralieFrV1, Main, Exploration, bibRecordById, PMC:4376448

Evidence for annexin A6-dependent plasma membrane remodelling of lipid domains

Identifieur interne : 002E36 ( Main/Exploration ); précédent : 002E35; suivant : 002E37

Evidence for annexin A6-dependent plasma membrane remodelling of lipid domains

Auteurs : Anna Alvarez-Guaita [Espagne] ; Sandra Vilà De Muga [Espagne] ; Dylan M. Owen [Australie] ; David Williamson [Australie] ; Astrid Magenau [Australie] ; Ana García-Melero [Espagne] ; Meritxell Reverter [Espagne] ; Monira Hoque [Australie] ; Rose Cairns [Australie] ; Rhea Cornely [Australie] ; Francesc Tebar [Espagne] ; Thomas Grewal [Australie] ; Katharina Gaus [Australie] ; Jesús Ayala-Sanmartín [France] ; Carlos Enrich [Espagne] ; Carles Rentero [Espagne]

Source :

British Journal of Pharmacology [ 0007-1188 ] ; 2015.

RBID : PMC:4376448

Abstract

Background and Purpose

Annexin A6 (AnxA6) is a calcium-dependent phospholipid-binding protein that can be recruited to the plasma membrane to function as a scaffolding protein to regulate signal complex formation, endo- and exocytic pathways as well as distribution of cellular cholesterol. Here, we have investigated how AnxA6 influences the membrane order.

Experimental Approach

We used Laurdan and di-4-ANEPPDHQ staining in (i) artificial membranes; (ii) live cells to investigate membrane packing and ordered lipid phases; and (iii) a super-resolution imaging (photoactivated localization microscopy, PALM) and Ripley's K second-order point pattern analysis approach to assess how AnxA6 regulates plasma membrane order domains and protein clustering.

Key Results

In artificial membranes, purified AnxA6 induced a global increase in membrane order. However, confocal microscopy using di-4-ANEPPDHQ in live cells showed that cells expressing AnxA6, which reduces plasma membrane cholesterol levels and modifies the actin cytoskeleton meshwork, displayed a decrease in membrane order (∼15 and 30% in A431 and MEF cells respectively). PALM data from Lck10 and Src15 membrane raft/non-raft markers revealed that AnxA6 expression induced clustering of both raft and non-raft markers. Altered clustering of Lck10 and Src15 in cells expressing AnxA6 was also observed after cholesterol extraction with methyl-β-cyclodextrin or actin cytoskeleton disruption with latrunculin B.

Conclusions and Implications

AnxA6-induced plasma membrane remodelling indicated that elevated AnxA6 expression decreased membrane order through the regulation of cellular cholesterol homeostasis and the actin cytoskeleton. This study provides the first evidence from live cells that support current models of annexins as membrane organizers.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4376448

DOI: 10.1111/bph.13022
PubMed: 25409976
PubMed Central: 4376448

Affiliations:

Australie, Espagne, France

Le document en format XML

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<author><name sortKey="Hoque, Monira" sort="Hoque, Monira" uniqKey="Hoque M" first="Monira" last="Hoque">Monira Hoque</name>
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<author><name sortKey="Tebar, Francesc" sort="Tebar, Francesc" uniqKey="Tebar F" first="Francesc" last="Tebar">Francesc Tebar</name>
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<author><name sortKey="Grewal, Thomas" sort="Grewal, Thomas" uniqKey="Grewal T" first="Thomas" last="Grewal">Thomas Grewal</name>
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<author><name sortKey="Gaus, Katharina" sort="Gaus, Katharina" uniqKey="Gaus K" first="Katharina" last="Gaus">Katharina Gaus</name>
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<author><name sortKey="Ayala Sanmartin, Jesus" sort="Ayala Sanmartin, Jesus" uniqKey="Ayala Sanmartin J" first="Jesús" last="Ayala-Sanmartín">Jesús Ayala-Sanmartín</name>
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<author><name sortKey="Rentero, Carles" sort="Rentero, Carles" uniqKey="Rentero C" first="Carles" last="Rentero">Carles Rentero</name>
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<series><title level="j">British Journal of Pharmacology</title>
<idno type="ISSN">0007-1188</idno>
<idno type="eISSN">1476-5381</idno>
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<front><div type="abstract" xml:lang="en"><sec><title>Background and Purpose</title>
<p>Annexin A6 (AnxA6) is a calcium-dependent phospholipid-binding protein that can be recruited to the plasma membrane to function as a scaffolding protein to regulate signal complex formation, endo- and exocytic pathways as well as distribution of cellular cholesterol. Here, we have investigated how AnxA6 influences the membrane order.</p>
</sec>
<sec><title>Experimental Approach</title>
<p>We used Laurdan and di-4-ANEPPDHQ staining in (i) artificial membranes; (ii) live cells to investigate membrane packing and ordered lipid phases; and (iii) a super-resolution imaging (photoactivated localization microscopy, PALM) and Ripley's K second-order point pattern analysis approach to assess how AnxA6 regulates plasma membrane order domains and protein clustering.</p>
</sec>
<sec><title>Key Results</title>
<p>In artificial membranes, purified AnxA6 induced a global increase in membrane order. However, confocal microscopy using di-4-ANEPPDHQ in live cells showed that cells expressing AnxA6, which reduces plasma membrane cholesterol levels and modifies the actin cytoskeleton meshwork, displayed a decrease in membrane order (∼15 and 30% in A431 and MEF cells respectively). PALM data from Lck10 and Src15 membrane raft/non-raft markers revealed that AnxA6 expression induced clustering of both raft and non-raft markers. Altered clustering of Lck10 and Src15 in cells expressing AnxA6 was also observed after cholesterol extraction with methyl-β-cyclodextrin or actin cytoskeleton disruption with latrunculin B.</p>
</sec>
<sec><title>Conclusions and Implications</title>
<p>AnxA6-induced plasma membrane remodelling indicated that elevated AnxA6 expression decreased membrane order through the regulation of cellular cholesterol homeostasis and the actin cytoskeleton. This study provides the first evidence from live cells that support current models of annexins as membrane organizers.</p>
</sec>
</div>
</front>
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<name sortKey="Reverter, Meritxell" sort="Reverter, Meritxell" uniqKey="Reverter M" first="Meritxell" last="Reverter">Meritxell Reverter</name>
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<name sortKey="Williamson, David" sort="Williamson, David" uniqKey="Williamson D" first="David" last="Williamson">David Williamson</name>
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<country name="France"><noRegion><name sortKey="Ayala Sanmartin, Jesus" sort="Ayala Sanmartin, Jesus" uniqKey="Ayala Sanmartin J" first="Jesús" last="Ayala-Sanmartín">Jesús Ayala-Sanmartín</name>
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   |wiki=    Wicri/Asie
   |area=    AustralieFrV1
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   |clé=     PMC:4376448
   |texte=   Evidence for annexin A6-dependent plasma membrane remodelling of lipid domains
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Serveur d'exploration sur les relations entre la France et l'Australie

Evidence for annexin A6-dependent plasma membrane remodelling of lipid domains

Evidence for annexin A6-dependent plasma membrane remodelling of lipid domains

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Abstract

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	Serveur d'exploration sur les relations entre la France et l'Australie
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