FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner

Research output: Contribution to journalJournal articlepeer-review

Standard

FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner. / Ramesh, Pradeep; Baroji, Younes F.; Seyyed Reihani, Seyyed Nader; Stamou, Dimitrios; Oddershede, Lene Broeng; Bendix, Pól Martin.

In: Scientific Reports, Vol. 3, 31.01.2013, p. 1565-(1-6).

Research output: Contribution to journalJournal articlepeer-review

Harvard

Ramesh, P, Baroji, YF, Seyyed Reihani, SN, Stamou, D, Oddershede, LB & Bendix, PM 2013, 'FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner', Scientific Reports, vol. 3, pp. 1565-(1-6). https://doi.org/10.1038/srep01565

APA

Ramesh, P., Baroji, Y. F., Seyyed Reihani, S. N., Stamou, D., Oddershede, L. B., & Bendix, P. M. (2013). FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner. Scientific Reports, 3, 1565-(1-6). https://doi.org/10.1038/srep01565

Vancouver

Ramesh P, Baroji YF, Seyyed Reihani SN, Stamou D, Oddershede LB, Bendix PM. FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner. Scientific Reports. 2013 Jan 31;3:1565-(1-6). https://doi.org/10.1038/srep01565

Author

Ramesh, Pradeep ; Baroji, Younes F. ; Seyyed Reihani, Seyyed Nader ; Stamou, Dimitrios ; Oddershede, Lene Broeng ; Bendix, Pól Martin. / FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner. In: Scientific Reports. 2013 ; Vol. 3. pp. 1565-(1-6).

Bibtex

@article{b21eb65bd4634624bbdfdb92a265500a,
title = "FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner",
abstract = "Syndapin 1 FBAR, a member of the Bin-amphiphysin-Rvs (BAR) domain protein family, is known to induce membrane curvature and is an essential component in biological processes like endocytosis and formation and growth of neurites. We quantify the curvature sensing of FBAR on reconstituted porcine brain lipid vesicles and show that it senses membrane curvature at low density whereas it induces and reinforces tube stiffness at higher density. FBAR strongly up-concentrates on the high curvature tubes pulled out of Giant Unilamellar lipid Vesicles (GUVs), this sorting behavior is strongly amplified at low protein densities. Interestingly, FBAR from syndapin 1 has a large affinity for tubular membranes with curvatures larger than its own intrinsic concave curvature. Finally, we studied the effect of FBAR on membrane relaxation kinetics with high temporal resolution and found that the protein increases relaxation time of the tube holding force in a density-dependent fashion.",
author = "Pradeep Ramesh and Baroji, {Younes F.} and {Seyyed Reihani}, {Seyyed Nader} and Dimitrios Stamou and Oddershede, {Lene Broeng} and Bendix, {P{\'o}l Martin}",
year = "2013",
month = jan,
day = "31",
doi = "10.1038/srep01565",
language = "English",
volume = "3",
pages = "1565--(1--6)",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent manner

AU - Ramesh, Pradeep

AU - Baroji, Younes F.

AU - Seyyed Reihani, Seyyed Nader

AU - Stamou, Dimitrios

AU - Oddershede, Lene Broeng

AU - Bendix, Pól Martin

PY - 2013/1/31

Y1 - 2013/1/31

N2 - Syndapin 1 FBAR, a member of the Bin-amphiphysin-Rvs (BAR) domain protein family, is known to induce membrane curvature and is an essential component in biological processes like endocytosis and formation and growth of neurites. We quantify the curvature sensing of FBAR on reconstituted porcine brain lipid vesicles and show that it senses membrane curvature at low density whereas it induces and reinforces tube stiffness at higher density. FBAR strongly up-concentrates on the high curvature tubes pulled out of Giant Unilamellar lipid Vesicles (GUVs), this sorting behavior is strongly amplified at low protein densities. Interestingly, FBAR from syndapin 1 has a large affinity for tubular membranes with curvatures larger than its own intrinsic concave curvature. Finally, we studied the effect of FBAR on membrane relaxation kinetics with high temporal resolution and found that the protein increases relaxation time of the tube holding force in a density-dependent fashion.

AB - Syndapin 1 FBAR, a member of the Bin-amphiphysin-Rvs (BAR) domain protein family, is known to induce membrane curvature and is an essential component in biological processes like endocytosis and formation and growth of neurites. We quantify the curvature sensing of FBAR on reconstituted porcine brain lipid vesicles and show that it senses membrane curvature at low density whereas it induces and reinforces tube stiffness at higher density. FBAR strongly up-concentrates on the high curvature tubes pulled out of Giant Unilamellar lipid Vesicles (GUVs), this sorting behavior is strongly amplified at low protein densities. Interestingly, FBAR from syndapin 1 has a large affinity for tubular membranes with curvatures larger than its own intrinsic concave curvature. Finally, we studied the effect of FBAR on membrane relaxation kinetics with high temporal resolution and found that the protein increases relaxation time of the tube holding force in a density-dependent fashion.

U2 - 10.1038/srep01565

DO - 10.1038/srep01565

M3 - Journal article

C2 - 23535634

VL - 3

SP - 1565-(1-6)

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

ER -

ID: 49100166