- Email: [email protected]
11 (2015) 1511–1520]
Biochimica et Biophysica Acta 1861 (2016) 68
Contents lists available at ScienceDirect
Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbalip
Corrigendum
Corrigendum to “G protein-membrane interactions I: Gαi1 myristoyl and palmitoyl modifications in protein–lipid interactions and its implications in membrane microdomain localization” [Biochim. Biophys. Acta 1851/11 (2015) 1511–1520] Rafael Alvarez a, David J. López a, Jesús Casas a, Victoria Lladó a, Mónica Higuera a, Tünde Nagya, Miquel Barceló b, Xavier Busquets a, Pablo V. Escribá a,⁎ a b
Laboratory of Molecular Cell Biomedicine, Department of Biology, IUNICS, University of Islas Baleares, Carretera de Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain Bioinorganic and Bioorganic Research Group, Department of Chemistry, IUNICS, University of Islas Baleares, Carretera de Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain
The authors would like to correct the Highlights of the abovereferenced article. The corrected version of Highlights appears below. • The Gαi1 protein has a permanent myristoyl and a reversible palmitoyl moiety. • Myristoyl and palmitoyl moieties regulate Gαi1 membrane microdomain localization.
DOI of original article: http://dx.doi.org/10.1016/j.bbalip.2015.08.001. ⁎ Corresponding author. E-mail address: [email protected] (P.V. Escribá).
http://dx.doi.org/10.1016/j.bbalip.2015.10.006 1388-1981/© 2015 Published by Elsevier B.V.
• Myristoylation favors Gαi1 protein localization to ordered lamellar membranes. • Gαi1 depalmitoylation increases its affinity to lamellar domains with negative charge. • Depalmitoylation induces Gαi1 basic amino acid exposure to the membrane surface.
Contents lists available at ScienceDirect
Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbalip
Corrigendum
Corrigendum to “G protein-membrane interactions I: Gαi1 myristoyl and palmitoyl modifications in protein–lipid interactions and its implications in membrane microdomain localization” [Biochim. Biophys. Acta 1851/11 (2015) 1511–1520] Rafael Alvarez a, David J. López a, Jesús Casas a, Victoria Lladó a, Mónica Higuera a, Tünde Nagya, Miquel Barceló b, Xavier Busquets a, Pablo V. Escribá a,⁎ a b
Laboratory of Molecular Cell Biomedicine, Department of Biology, IUNICS, University of Islas Baleares, Carretera de Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain Bioinorganic and Bioorganic Research Group, Department of Chemistry, IUNICS, University of Islas Baleares, Carretera de Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain
The authors would like to correct the Highlights of the abovereferenced article. The corrected version of Highlights appears below. • The Gαi1 protein has a permanent myristoyl and a reversible palmitoyl moiety. • Myristoyl and palmitoyl moieties regulate Gαi1 membrane microdomain localization.
DOI of original article: http://dx.doi.org/10.1016/j.bbalip.2015.08.001. ⁎ Corresponding author. E-mail address: [email protected] (P.V. Escribá).
http://dx.doi.org/10.1016/j.bbalip.2015.10.006 1388-1981/© 2015 Published by Elsevier B.V.
• Myristoylation favors Gαi1 protein localization to ordered lamellar membranes. • Gαi1 depalmitoylation increases its affinity to lamellar domains with negative charge. • Depalmitoylation induces Gαi1 basic amino acid exposure to the membrane surface.