Locally resolved membrane binding affinity of the N-terminus of α-synuclein

Marta Robotta; Christian Hintze; Stefan Schildknecht; Niels Zijlstra; Christian Jüngst; Christiaan Karreman; Martina Huber; Marcel Leist; Vinod Subramaniam; Malte Drescher

doi:10.1021/bi300357a

Locally resolved membrane binding affinity of the N-terminus of α-synuclein

Marta Robotta
, Christian Hintze
, Stefan Schildknecht
, Niels Zijlstra
, Christian Jüngst
, Christiaan Karreman
, Martina Huber
, Marcel Leist
, Vinod Subramaniam
, Malte Drescher

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein-membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.

Original language	English
Pages (from-to)	3960-2
Number of pages	3
Journal	Biochemistry
Volume	51
Issue number	19
DOIs	https://doi.org/10.1021/bi300357a
Publication status	Published - 2012

Keywords

Cell Membrane
Electron Spin Resonance Spectroscopy
Humans
Lewy Bodies
Membranes, Artificial
Mutation
Phosphatidylcholines
Phosphatidylglycerols
Phospholipids
alpha-Synuclein
Journal Article
Research Support, Non-U.S. Gov't

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10.1021/bi300357a

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title = "Locally resolved membrane binding affinity of the N-terminus of α-synuclein",

abstract = "α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein-membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.",

keywords = "Cell Membrane, Electron Spin Resonance Spectroscopy, Humans, Lewy Bodies, Membranes, Artificial, Mutation, Phosphatidylcholines, Phosphatidylglycerols, Phospholipids, alpha-Synuclein, Journal Article, Research Support, Non-U.S. Gov't",

author = "Marta Robotta and Christian Hintze and Stefan Schildknecht and Niels Zijlstra and Christian J{\"u}ngst and Christiaan Karreman and Martina Huber and Marcel Leist and Vinod Subramaniam and Malte Drescher",

year = "2012",

doi = "10.1021/bi300357a",

language = "English",

volume = "51",

pages = "3960--2",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "19",

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TY - JOUR

T1 - Locally resolved membrane binding affinity of the N-terminus of α-synuclein

AU - Robotta, Marta

AU - Hintze, Christian

AU - Schildknecht, Stefan

AU - Zijlstra, Niels

AU - Jüngst, Christian

AU - Karreman, Christiaan

AU - Huber, Martina

AU - Leist, Marcel

AU - Subramaniam, Vinod

AU - Drescher, Malte

PY - 2012

Y1 - 2012

N2 - α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein-membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.

AB - α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein-membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform.

KW - Cell Membrane

KW - Electron Spin Resonance Spectroscopy

KW - Humans

KW - Lewy Bodies

KW - Membranes, Artificial

KW - Mutation

KW - Phosphatidylcholines

KW - Phosphatidylglycerols

KW - Phospholipids

KW - alpha-Synuclein

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

UR - https://www.scopus.com/pages/publications/84861141891

UR - https://www.scopus.com/pages/publications/84861141891#tab=citedBy

U2 - 10.1021/bi300357a

DO - 10.1021/bi300357a

M3 - Article

C2 - 22494024

SN - 0006-2960

VL - 51

SP - 3960

EP - 3962

JO - Biochemistry

JF - Biochemistry

IS - 19

ER -

Locally resolved membrane binding affinity of the N-terminus of α-synuclein

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Keywords

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