Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.

It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recogniz...

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Autores principales:	Marcin Wolny, Michał Grzybek, Ewa Bok, Anna Chorzalska, Marc Lenoir, Aleksander Czogalla, Klaudia Adamczyk, Adam Kolondra, Witold Diakowski, Michael Overduin, Aleksander F Sikorski
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d6183a326f1448a4a8b02f66308cdcc0
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spelling	oai:doaj.org-article:d6183a326f1448a4a8b02f66308cdcc02021-11-18T06:51:06ZKey amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.1932-620310.1371/journal.pone.0021538https://doaj.org/article/d6183a326f1448a4a8b02f66308cdcc02011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21738695/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recognizing monolayers and bilayers composed of PE/PC mixtures. In vitro binding studies revealed that a quadruple mutant with substituted hydrophobic residues W1771, L1775, M1778 and W1779 not only failed to effectively bind PE/PC, but its residual PE/PC-binding activity was insensitive to inhibition with ankyrin. Structure prediction and analysis, supported by in vitro experiments, suggests that "opening" of the coiled-coil structure underlies the mechanism of this interaction. Experiments on red blood cells and HeLa cells supported the conclusions derived from the model and in vitro lipid-protein interaction results, and showed the potential physiological role of this binding. We postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton.Marcin WolnyMichał GrzybekEwa BokAnna ChorzalskaMarc LenoirAleksander CzogallaKlaudia AdamczykAdam KolondraWitold DiakowskiMichael OverduinAleksander F SikorskiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 6, p e21538 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marcin Wolny Michał Grzybek Ewa Bok Anna Chorzalska Marc Lenoir Aleksander Czogalla Klaudia Adamczyk Adam Kolondra Witold Diakowski Michael Overduin Aleksander F Sikorski Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
description	It was shown previously that an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine (PE/PC) binding site maps to the N-terminal part of the ankyrin-binding domain of β-spectrin (ankBDn). Here we have identified the amino acid residues within this domain which are responsible for recognizing monolayers and bilayers composed of PE/PC mixtures. In vitro binding studies revealed that a quadruple mutant with substituted hydrophobic residues W1771, L1775, M1778 and W1779 not only failed to effectively bind PE/PC, but its residual PE/PC-binding activity was insensitive to inhibition with ankyrin. Structure prediction and analysis, supported by in vitro experiments, suggests that "opening" of the coiled-coil structure underlies the mechanism of this interaction. Experiments on red blood cells and HeLa cells supported the conclusions derived from the model and in vitro lipid-protein interaction results, and showed the potential physiological role of this binding. We postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton.
format	article
author	Marcin Wolny Michał Grzybek Ewa Bok Anna Chorzalska Marc Lenoir Aleksander Czogalla Klaudia Adamczyk Adam Kolondra Witold Diakowski Michael Overduin Aleksander F Sikorski
author_facet	Marcin Wolny Michał Grzybek Ewa Bok Anna Chorzalska Marc Lenoir Aleksander Czogalla Klaudia Adamczyk Adam Kolondra Witold Diakowski Michael Overduin Aleksander F Sikorski
author_sort	Marcin Wolny
title	Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
title_short	Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
title_full	Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
title_fullStr	Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
title_full_unstemmed	Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.
title_sort	key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βi-spectrin.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/d6183a326f1448a4a8b02f66308cdcc0
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Key amino acid residues of ankyrin-sensitive phosphatidylethanolamine/phosphatidylcholine-lipid binding site of βI-spectrin.

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