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.
authors.affiliation: Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 Copenhagen, Denmark.
authors.forename: Pradeep
authors.initials: P
authors.lastname: Ramesh
authors.forename: Younes F
authors.initials: YF
authors.lastname: Baroji
authors.forename: S Nader S
authors.initials: SN
authors.lastname: Reihani
authors.forename: Dimitrios
authors.initials: D
authors.lastname: Stamou
authors.forename: Lene B
authors.initials: LB
authors.lastname: Oddershede
authors.forename: Poul Martin
authors.initials: PM
authors.lastname: Bendix
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D022162:Cytoplasmic Vesicles / Q000378:metabolism; D004705:Endocytosis; D008081:Liposomes / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009479:Neuropeptides / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013552:Swine; D053835:Unilamellar Liposomes / Q000378:metabolism*
chemical_list: D008081:Liposomes; D009419:Nerve Tissue Proteins; D009479:Neuropeptides; D010750:Phosphoproteins; D053835:Unilamellar Liposomes; C075637:amphiphysin
references.citation: EMBO J. 2009 Nov 4;28(21):3303-14
references.pmid: 19816406
references.citation: Int J Biochem Mol Biol. 2012;3(2):198-208
references.pmid: 22773959
references.citation: J Phys Chem Lett. 2010 Nov 16;1(23):3401-3406
references.pmid: 23772271
references.citation: Biophys Chem. 2008 Sep;137(1):7-12
references.pmid: 18602207
references.citation: Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):12700-5
references.pmid: 19549836
references.citation: Science. 2004 Jan 23;303(5657):495-9
references.pmid: 14645856
references.citation: Nano Lett. 2011 Dec 14;11(12):5431-7
references.pmid: 22074221
references.citation: Nano Lett. 2005 Oct;5(10):1937-42
references.pmid: 16218713
references.citation: Phys Rev E Stat Nonlin Soft Matter Phys. 2012 May;85(5 Pt 1):051906
references.pmid: 23004787
references.citation: J Neurosci. 2009 Oct 21;29(42):13315-27
references.pmid: 19846719
references.citation: Biophys J. 1991 Apr;59(4):775-85
references.pmid: 2065185
references.citation: Cell. 2008 Mar 7;132(5):807-17
references.pmid: 18329367
references.citation: Annu Rev Phys Chem. 2011;62:483-506
references.pmid: 21219150
references.citation: Nature. 2005 Dec 1;438(7068):590-6
references.pmid: 16319878
references.citation: Cell Mol Life Sci. 2011 Dec;68(24):3983-93
references.pmid: 21769645
references.citation: Annu Rev Biochem. 2011;80:101-23
references.pmid: 21438688
references.citation: Structure. 2007 Jul;15(7):839-52
references.pmid: 17540576
references.citation: PLoS One. 2009 Dec 03;4(12):e8150
references.pmid: 19997509
references.citation: Biophys J. 2009 Apr 8;96(7):2676-88
references.pmid: 19348750
references.citation: Proc Natl Acad Sci U S A. 2010 Mar 2;107(9):4141-6
references.pmid: 20160074
references.citation: Phys Rev E Stat Nonlin Soft Matter Phys. 2011 Jan;83(1 Pt 1):011905
references.pmid: 21405711
references.citation: Biophys J. 1996 Dec;71(6):3242-50
references.pmid: 8968594
references.citation: Biophys J. 2012 Apr 18;102(8):1837-45
references.pmid: 22768939
references.citation: Phys Rev Lett. 2002 Jun 10;88(23):238101
references.pmid: 12059401
references.citation: J Biol Chem. 2012 Jun 22;287(26):22387-96
references.pmid: 22573331
references.citation: Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):173-8
references.pmid: 22184226
references.citation: Proc Natl Acad Sci U S A. 2010 May 4;107(18):8213-8
references.pmid: 20404169
references.citation: J Biol Chem. 2006 May 12;281(19):13285-13299
references.pmid: 16540475
references.citation: Mol Biol Cell. 1999 Feb;10(2):501-13
references.pmid: 9950691
references.citation: Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5622-6
references.pmid: 19304798
references.citation: Biophys J. 1982 Jul;39(1):71-81
references.pmid: 7104453
references.citation: Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics. 1993 Sep;48(3):R1642-R1645
references.pmid: 9960868