Dynamics of membrane nanotubes coated with I-BAR

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Standard

Dynamics of membrane nanotubes coated with I-BAR. / Farhangibarooji, Younes; Rørvig-Lund, Andreas; Semsey, Szabolcs; S. Reihani, S. Nader; Bendix, Pól Martin.

I: Scientific Reports, Bind 6, 30054, 2016.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Farhangibarooji, Y, Rørvig-Lund, A, Semsey, S, S. Reihani, SN & Bendix, PM 2016, 'Dynamics of membrane nanotubes coated with I-BAR', Scientific Reports, bind 6, 30054. https://doi.org/10.1038/srep30054

APA

Farhangibarooji, Y., Rørvig-Lund, A., Semsey, S., S. Reihani, S. N., & Bendix, P. M. (2016). Dynamics of membrane nanotubes coated with I-BAR. Scientific Reports, 6, [30054]. https://doi.org/10.1038/srep30054

Vancouver

Farhangibarooji Y, Rørvig-Lund A, Semsey S, S. Reihani SN, Bendix PM. Dynamics of membrane nanotubes coated with I-BAR. Scientific Reports. 2016;6. 30054. https://doi.org/10.1038/srep30054

Author

Farhangibarooji, Younes ; Rørvig-Lund, Andreas ; Semsey, Szabolcs ; S. Reihani, S. Nader ; Bendix, Pól Martin. / Dynamics of membrane nanotubes coated with I-BAR. I: Scientific Reports. 2016 ; Bind 6.

Bibtex

@article{d80709f4f8254a11aa9d4e9cf85c7b0e,
title = "Dynamics of membrane nanotubes coated with I-BAR",
abstract = "Membrane deformation is a necessary step in a number of cellular processes such as filopodia and invadopodia formation and has been shown to involve membrane shaping proteins containing membrane binding domains from the IRSp53-MIM protein family. In reconstituted membranes the membrane shaping domains can efficiently deform negatively charged membranes into tubules without any other proteins present. Here, we show that the IM domain (also called I-BAR domain) from the protein ABBA, forms semi-flexible nanotubes protruding into Giant Unilamellar lipid Vesicles (GUVs). By simultaneous quantification of tube intensity and tubular shape we find both the diameter and stiffness of the nanotubes. I-BAR decorated tubes were quantified to have a diameter of ~50 nm and exhibit no stiffening relative to protein free tubes of the same diameter. At high protein density the tubes are immobile whereas at lower density the tubes diffuse freely on the surface of the GUV. Bleaching experiments of the fluorescently tagged I-BAR confirmed that the mobility of the tubes correlates with the mobility of the I-BAR on the GUV membrane. Finally, at low density of I-BAR the protein upconcentrates within tubes protruding into the GUVs. This implies that I-BAR exhibits strong preference for negatively curved membranes.",
keywords = "Journal Article",
author = "Younes Farhangibarooji and Andreas R{\o}rvig-Lund and Szabolcs Semsey and {S. Reihani}, {S. Nader} and Bendix, {P{\'o}l Martin}",
year = "2016",
doi = "10.1038/srep30054",
language = "English",
volume = "6",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Dynamics of membrane nanotubes coated with I-BAR

AU - Farhangibarooji, Younes

AU - Rørvig-Lund, Andreas

AU - Semsey, Szabolcs

AU - S. Reihani, S. Nader

AU - Bendix, Pól Martin

PY - 2016

Y1 - 2016

N2 - Membrane deformation is a necessary step in a number of cellular processes such as filopodia and invadopodia formation and has been shown to involve membrane shaping proteins containing membrane binding domains from the IRSp53-MIM protein family. In reconstituted membranes the membrane shaping domains can efficiently deform negatively charged membranes into tubules without any other proteins present. Here, we show that the IM domain (also called I-BAR domain) from the protein ABBA, forms semi-flexible nanotubes protruding into Giant Unilamellar lipid Vesicles (GUVs). By simultaneous quantification of tube intensity and tubular shape we find both the diameter and stiffness of the nanotubes. I-BAR decorated tubes were quantified to have a diameter of ~50 nm and exhibit no stiffening relative to protein free tubes of the same diameter. At high protein density the tubes are immobile whereas at lower density the tubes diffuse freely on the surface of the GUV. Bleaching experiments of the fluorescently tagged I-BAR confirmed that the mobility of the tubes correlates with the mobility of the I-BAR on the GUV membrane. Finally, at low density of I-BAR the protein upconcentrates within tubes protruding into the GUVs. This implies that I-BAR exhibits strong preference for negatively curved membranes.

AB - Membrane deformation is a necessary step in a number of cellular processes such as filopodia and invadopodia formation and has been shown to involve membrane shaping proteins containing membrane binding domains from the IRSp53-MIM protein family. In reconstituted membranes the membrane shaping domains can efficiently deform negatively charged membranes into tubules without any other proteins present. Here, we show that the IM domain (also called I-BAR domain) from the protein ABBA, forms semi-flexible nanotubes protruding into Giant Unilamellar lipid Vesicles (GUVs). By simultaneous quantification of tube intensity and tubular shape we find both the diameter and stiffness of the nanotubes. I-BAR decorated tubes were quantified to have a diameter of ~50 nm and exhibit no stiffening relative to protein free tubes of the same diameter. At high protein density the tubes are immobile whereas at lower density the tubes diffuse freely on the surface of the GUV. Bleaching experiments of the fluorescently tagged I-BAR confirmed that the mobility of the tubes correlates with the mobility of the I-BAR on the GUV membrane. Finally, at low density of I-BAR the protein upconcentrates within tubes protruding into the GUVs. This implies that I-BAR exhibits strong preference for negatively curved membranes.

KW - Journal Article

U2 - 10.1038/srep30054

DO - 10.1038/srep30054

M3 - Journal article

C2 - 27444356

VL - 6

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 30054

ER -

ID: 178251616