Phospholipid-induced structural changes to an erythroid beta spectrin ankyrin-dependent lipid-binding site

Biochimica Et Biophysica Acta
Aleksander CzogallaAleksander F Sikorski

Abstract

The region of beta-spectrin that is responsible for interactions with ankyrin was shown to comprise an ankyrin-sensitive lipid-binding site. Structural studies indicate that it exhibits a mixed 3(10)/alpha helical conformation and is highly amphipathic. These features together with the distinctively conserved sequence of the lipid-binding site motivated us to explore the mechanism of its interactions with biological membranes. A series of singly and doubly spin-labeled erythroid beta-spectrin-derived peptides was constructed, and the spin-label mobility and spin-spin distances were analyzed via electron paramagnetic resonance spectroscopy and two different calculation methods. The results indicate that in beta-spectrin, the lipid-binding domain, which is part of the 14(th) segment, has the topology of typical triple-helical spectrin repeat. However, it undergoes significant changes when interacting with phospholipids or detergents. A mechanism for these interactions is proposed in this paper.

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May 24, 2007·Molecular Membrane Biology·Aleksander CzogallaAleksander F Sikorski

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Citations

Apr 23, 2010·Cellular and Molecular Life Sciences : CMLS·Aleksander Czogalla, Aleksander F Sikorski
May 16, 2012·FEBS Letters·Elisabeth Le RumeurSteve J Winder
Dec 5, 2013·Science China. Life Sciences·Rui ZhangDongHai Li
May 16, 2013·Biochimica Et Biophysica Acta·Beata MachnickaAleksander F Sikorski
Jan 21, 2010·Physiological Reviews·Juha SaarikangasPekka Lappalainen
Feb 27, 2014·Cellular & Molecular Biology Letters·Dżamila M BogusławskaAleksander Czogalla
Apr 2, 2020·Materials Science & Engineering. C, Materials for Biological Applications·Róbert DeákZoltán Varga

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