Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein

被引:56
|
作者
Robotta, Marta [4 ]
Braun, Patrick [4 ]
van Rooijen, Bart [1 ,2 ]
Subramaniam, Vinod [1 ,2 ]
Huber, Martina [3 ]
Drescher, Malte [4 ]
机构
[1] Univ Twente, MESA Inst Nanotechnol, NL-7500 AE Enschede, Netherlands
[2] Univ Twente, MIRA Inst Biomed Technol & Tech Med, NL-7500 AE Enschede, Netherlands
[3] Leiden Univ, Leiden Inst Phys, NL-2300 RA Leiden, Netherlands
[4] Univ Konstanz, Dept Chem, D-78457 Constance, Germany
关键词
electron paramagnetic resonance; membranes; proteins; site-directed spin labeling; vesicles; DYNAMICS; BINDING; PROTEIN; VESICLES; DISEASE;
D O I
10.1002/cphc.201000815
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Good luck! The physiologically relevant conformation of membrane-bound α-Synuclein (αS) can be either a horseshoe or an extended helix structure. Experimental data obtained by site-directed spin labeling in combination with pulsed electron paramagnetic resonance provide compelling evidence of the coexistence of the horseshoe structure and an extended helix of αS bound to a membrane surface, and potentially resolve the debate on the structure of membrane-bound αS. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:267 / 269
页数:3
相关论文
共 31 条
  • [21] Parkinson's disease-associated mutants shift equilibrium bound state of alpha-synuclein towards the second helix
    Maltseva, Sofiya
    Kerr, Daniel H.
    Turke, Miah J.
    Lee, Ka Yee C.
    BIOPHYSICAL JOURNAL, 2023, 122 (03) : 342A - 342A
  • [22] Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations
    Dikiy, Igor
    Fauvet, Bruno
    Jovicic, Ana
    Mahul-Mellier, Anne-Laure
    Desobry, Carole
    El-Turk, Farah
    Gitler, Aaron D.
    Lashuel, Hilal A.
    Eliezer, David
    ACS CHEMICAL BIOLOGY, 2016, 11 (09) : 2428 - 2437
  • [23] alpha-synuclein inhibits Snx3-retromer retrograde trafficking of the conserved membrane-bound proprotein convertase Kex2 in the secretory pathway of Saccharomyces cerevisiae
    Rajasekaran, Santhanasabapathy
    Peterson, Patricia P.
    Liu, Zhengchang
    Robinson, Lucy C.
    Witt, Stephan N.
    HUMAN MOLECULAR GENETICS, 2022, 31 (05) : 705 - 717
  • [24] Interaction of native and partially folded conformations of alpha-lactalbumin with lipid bilayers: Characterization of two membrane-bound states
    Banuelos, S
    Muga, A
    FEBS LETTERS, 1996, 386 (01): : 21 - 25
  • [25] CONFORMATIONS OF YEAST ALPHA-MATING FACTOR AND ANALOG PEPTIDES AS BOUND TO PHOSPHOLIPID-BILAYER - CORRELATION OF MEMBRANE-BOUND CONFORMATION WITH PHYSIOLOGICAL-ACTIVITY
    WAKAMATSU, K
    OKADA, A
    MIYAZAWA, T
    MASUI, Y
    SAKAKIBARA, S
    HIGASHIJIMA, T
    EUROPEAN JOURNAL OF BIOCHEMISTRY, 1987, 163 (02): : 331 - 338
  • [26] PHYSIOLOGICAL ACTIVITIES OF PEPTIDES ARE CORRELATED WITH THE CONFORMATIONS OF MEMBRANE-BOUND MOLECULES - ALPHA-MATING FACTOR FROM SACCHAROMYCES-CEREVISIAE AND ANALOG PEPTIDES
    HIGASHIJIMA, T
    FUJIMURA, K
    MASUI, Y
    SAKAKIBARA, S
    MIYAZAWA, T
    FEBS LETTERS, 1983, 159 (1-2) : 229 - 232
  • [27] Solution and Membrane-Bound Conformations of the Tandem C2A and C2B Domains of Synaptotagmin 1: Evidence for Bilayer Bridging
    Herrick, Dawn Z.
    Kuo, Weiwei
    Huang, Hao
    Schwieters, Charles D.
    Ellena, Jeffrey F.
    Cafiso, David S.
    JOURNAL OF MOLECULAR BIOLOGY, 2009, 390 (05) : 913 - 923
  • [28] Solid-state nuclear magnetic resonance evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion peptide
    Yang, J
    Gabrys, CM
    Weliky, DP
    BIOCHEMISTRY, 2001, 40 (27) : 8126 - 8137
  • [29] 4-4-20-ANTI-FLUORESCYL IGG FAB' RECOGNITION OF MEMBRANE-BOUND HAPTEN - DIRECT EVIDENCE FOR THE ROLE OF PROTEIN AND INTERFACIAL STRUCTURE
    LECKBAND, DE
    KUHL, T
    WANG, HK
    HERRON, J
    MULLER, W
    RINGSDORF, H
    BIOCHEMISTRY, 1995, 34 (36) : 11467 - 11478
  • [30] FOURIER-TRANSFORM INFRARED EVIDENCE FOR A PREDOMINANTLY ALPHA-HELICAL STRUCTURE OF THE MEMBRANE-BOUND CHANNEL FORMING COOH-TERMINAL PEPTIDE OF COLICIN E1
    RATH, P
    BOUSCHE, O
    MERRILL, AR
    CRAMER, WA
    ROTHSCHILD, KJ
    BIOPHYSICAL JOURNAL, 1991, 59 (03) : 516 - 522