Lipid organization regulates annexin A2 Ca2+-sensitivity for membrane bridging and its modulator effects on membrane fluidity

Autor: Françoise Illien, Marine Coué, Chiara di Marco, Jesus Ayala-Sanmartin, Hong-Rong Piao
Přispěvatelé: Centre de Recherche Saint-Antoine (UMRS893), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Pierre et Marie Curie - Paris 6 (UPMC), Ayala-Sanmartin, Jesus, École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL), Bush Estate, Centre for Ecology and Hydrology, École Pratique des Hautes Études (EPHE)
Rok vydání: 2012
Předmět:
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Antiporter
Biophysics
[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Biochemistry
Exocytosis
Anionic phospholipid
03 medical and health sciences
Membrane domains
[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Membrane fluidity
Animals
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Lipid raft
Cells
Cultured
Annexin A2
030304 developmental biology
0303 health sciences
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
[CHIM.ORGA]Chemical Sciences/Organic chemistry
Chemistry
030302 biochemistry & molecular biology
Peripheral membrane protein
Biological membrane
Cell Biology
Lipid Metabolism
Cell biology
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
Spectrometry
Fluorescence
Cholesterol
Membrane
Anionic phospholipids
Membrane domain
Cattle
Calcium
Zdroj: BBA-Biochimica et Biophysica Acta
BBA-Biochimica et Biophysica Acta, 2012, 1818 (11), pp.2892-2900. ⟨10.1016/j.bbamem.2012.07.012⟩
BBA-Biochimica et Biophysica Acta, Elsevier, 2012, 1818 (11), pp.2892-2900. ⟨10.1016/j.bbamem.2012.07.012⟩
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2012
Biochimica et Biophysica Acta:Biomembranes, 2012
ISSN: 0005-2736
0006-3002
1879-2642
DOI: 10.1016/j.bbamem.2012.07.012
Popis: International audience; Annexin A2 (AnxA2) is a phospholipid binding protein that has been implicated in many membrane-related cellular functions. AnxA2 is able to bind different acidic phospholipids such as phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PI2P). This binding is mediated by Ca(2+)-dependent and Ca(2+)-independent mechanisms. The specific functions of annexin A2 related to these two phospholipids and the molecular mechanisms involved in their interaction remain obscure. Herein we studied the influence of lipid composition on the Ca(2+)-dependency of AnxA2-mediated membrane bridging and on membrane fluidity. Membrane models of ten different lipid compositions and detergent-resistant membranes from two cellular sources were investigated. The results show that the AnxA2-mediated membrane bridging requires 3 to 50 times less calcium for PS-membranes than for PI2P-membranes. Membrane fluidity was measured by the ratiometric fluorescence parameter generalized polarization method with two fluorescent probes. Compared to controls containing low phospholipid ligand, AnxA2 was found to reduce the membrane fluidity of PI2P-membranes twice as much as the PS-membranes in the presence of calcium. On the contrary, at mild acidic pH in the absence of calcium AnxA2 reduces the fluidity of the PS-membranes more than the PI2P-membranes. The presence of cholesterol on the bilayer reduced the AnxA2 capacity to reduce membrane fluidity. The presented data shed light on the specific roles of PI2P, PS and cholesterol present on membranes related to the action of annexin A2 as a membrane bridging molecule during exocytosis and endocytosis events and as a plasma membrane domain phospholipid packing regulator.
Databáze: OpenAIRE
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