The Peripheral Binding of 14-3-3 gamma to Membranes Involves Isoform-Specific Histidine Residues
Por:
Bustad H.J., Skjaerven L., Ying M., Halskau, O, Baumann A., Rodriguez-Larrea D., Costas M., Underhaug J., Sanchez-Ruiz J.M., Martinez A.
Publicada:
26 nov 2012
Resumen:
Mammalian 14-3-3 protein scaffolds include seven conserved isoforms that bind numerous phosphorylated protein partners and regulate many cellular processes. Some 14-3-3-isoforms, notably gamma, have elevated affinity for membranes, which might contribute to modulate the subcellular localization of the partners and substantiate the importance of investigating molecular mechanisms of membrane interaction. By applying surface plasmon resonance we here show that the binding to phospholipid bilayers is stimulated when 14-3-3 gamma is complexed with its partner, a peptide corresponding to the Ser19-phosphorylated N-terminal region of tyrosine hydroxylase. Moreover, membrane interaction is dependent on salts of kosmotropic ions, which also stabilize 14-3-3 gamma. Electrostatic analysis of available crystal structures of gamma and of the non-membrane-binding zeta-isoform, complemented with molecular dynamics simulations, indicate that the electrostatic potential distribution of phosphopeptide-
Filiaciones:
Univ Nacl Autonoma Mexico, Fac Quim, Dept Quim Fis, Lab Biofis Quim, Mexico City 04510, DF, Mexico
Department of Biomedicine, University of Bergen, Bergen, Norway
Facultad de Ciencias, Departamento de Química Física, Universidad de Granada, Granada, Spain
Department of Chemistry, University of Oxford, Oxford, United Kingdom
All Open Access, Gold
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