Spontaneous insertion and partitioning of alkaline phosphatase into model lipid rafts

Milhiet, Pierre-Emmanuel; Giocondi, Marie-Cécile; Baghdadi, Omid; Ronzon, Frédéric; Roux, B.; Grimellec, Christian Le

doi:10.1093/embo-reports/kvf096

Cited by 139 publications

(148 citation statements)

References 28 publications

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“…For all samples, AFM showed that BIAP spontaneously inserted in the gel, i.e. highly ordered, phase of bilayers [67,68,40]. This spontaneous BIAP insertion into SLBs was in accordance with the observations reported for the insertion of various GPI proteins into biomembranes (see above).…”

Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 91%

“…Such homogeneous protein distribution was in accordance with the existence of a lateral diffusion only modestly reduced in l o phase as compared to the l d phase [2]. This effect of Chl in enhancing the insertion of BIAP, which also resulted in an increase of the ordered domains size, was further demonstrated by adding Chl-loaded methyl-β-cyclodextrin complexes to DOPC/SM bilayers incubated with the protein [68]. As mentioned earlier, POPC/SM/Chl ternary mixtures are more relevant to the composition of biomembrane domains than DOPC/SM/Chl.…”

Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 74%

“…For PLAP introduced in the liposomes before fusion with the mica (SLB b s), the protein was visualized practically exclusively (92%) in the SM/Chl enriched l o domains of DOPC/SM/ Chl (1:1:1, mol:mol) [82]. A similar conclusion was reached for BIAP inserted in l o domains of DOPC/SM/ Chl (1:1:0.35, mol:mol) SLB a s [68]. The presence of Chl in the lipid mixture was shown to markedly increase the quantitative insertion of BIAP.…”

Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 54%

“…Direct AFM detection of the AP-GPI presence on SLBs can be obtained upon addition of BIAP in the buffer bathing preformed ordered-fluid phase separated bilayers [40,68]. This is illustrated in Fig.…”

Section: Afm Detection Of Ap-gpi In Model Membranesmentioning

confidence: 99%

“…Direct visualization of AP-GPI dimers and aggregates inserted in membrane domains was reported both for samples where the protein was added after the SLBs formation (SLB a s) and for samples in which the protein was inserted during the formation of the liposomes (SLB b s), before the SLBs formation by fusion of the proteincontaining vesicles [18,40,68,82]. Two categories of SLBs under fluid-ordered phase separation have been examined by AFM.…”

Section: Afm Detection Of Ap-gpi In Model Membranesmentioning

confidence: 99%

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Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Giocondi

Seantier

Dosset

et al. 2007

Pflugers Arch - Eur J Physiol

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In plasma membranes, most glycosylphosphatidylinositol-anchored proteins (GPI proteins) would be associated with ordered microdomains enriched in sphingolipids and cholesterol. Debates on the composition and the nano-or mesoscales organization of these membrane domains are still opened. This complexity of biomembranes explains the use, in the recent years, of both model systems and atomic force microscopy (AFM) approaches to better characterize GPI proteins/membranes interactions. So far, the studies have mainly been focused on alkaline phosphatases of intestinal (BIAP) or placental (PLAP) origins reconstituted in model systems. The data show that GPI-anchored alkaline phosphatases (AP-GPI) molecules inserted in supported membranes can be easily imaged by AFM, in physiological buffer. They are generally observed in the most ordered domains of model membranes under phase separation, i.e. presenting both fluid and ordered domains. This direct access to the membrane structure at a mesoscopic scale allows establishing the GPI protein induced changes in microdomains size. It provides direct evidence for the temperature-dependent distribution of a GPI protein between fluid and ordered membrane domains. Origins of reported differences in the behavior of BIAP and PLAP are discussed. Finally, advantages and limits of AFM in the study of GPI proteins/membrane domains interactions are presented in this review.

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Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 91%

Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 74%

Section: Interaction Of Ap-gpi With Ordered Gel Domainssupporting

confidence: 54%

Section: Afm Detection Of Ap-gpi In Model Membranesmentioning

confidence: 99%

Section: Afm Detection Of Ap-gpi In Model Membranesmentioning

confidence: 99%

See 3 more Smart Citations

Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Giocondi

Seantier

Dosset

et al. 2007

Pflugers Arch - Eur J Physiol

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Recent Progress in the Application of Atomic Force Microscopy for Supported Lipid Bilayers

Zhong

2012

Chemistry A European J

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In the past two decades, atomic force microscopy has been widely used for studying supported lipid bilayer related research, including the structure and dynamics of membranes and membrane proteins, and the interaction of membranes with chemical and biological molecules. The focus of this minireview is on the recent progress in the application of atomic force microscopy for supported lipid bilayers. Such progress mainly includes the application in the following aspects: submolecular-resolution imaging, in situ observation, and nanomechanics measurement.

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Tritium labelling of a cholesterol amphiphile designed for cell membrane anchoring of proteins

Schäfer

Orbán

Kele

et al. 2015

Labelled Comp Radiopharmac

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Cell membrane association of proteins can be achieved by the addition of lipid moieties to the polypeptide chain, and such lipid-modified proteins have important biological functions. A class of cell surface proteins contains a complex glycosylphosphatidylinositol (GPI) glycolipid at the C-terminus, and they are accumulated in cholesterol-rich membrane microdomains, i.e. lipid rafts. Semisynthetic lipoproteins prepared from recombinant proteins and designed lipids are valuable probes and model systems of the membrane-associated proteins. Because GPI-anchored proteins can be reinserted into the cell membrane with the retention of the biological function, they are appropriate candidates for preparing models via reduction of the structural complexity. A synthetic headgroup was added to the 3β-hydroxyl group of cholesterol, an essential lipid component of rafts, and the resulting cholesterol derivative was used as a simplified GPI mimetic. In order to quantitate the membrane integrated GPI mimetic after the exogenous addition to live cells, a tritium labeled cholesterol anchor was prepared.The radioactive label was introduced into the headgroup, and the radiolabeled GPI mimetic anchor was obtained with a specific activity of 1.37 TBq/mmol. The headgroup labeled cholesterol derivative was applied to demonstrate the sensitive detection of the cell membrane association of the anchor under in vivo conditions.

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Spontaneous insertion and partitioning of alkaline phosphatase into model lipid rafts

Cited by 139 publications

References 28 publications

Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Recent Progress in the Application of Atomic Force Microscopy for Supported Lipid Bilayers

Tritium labelling of a cholesterol amphiphile designed for cell membrane anchoring of proteins

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