Publication:
Tyrosine phosphorylation of the inactivating peptide of the Shaker B potassium channel: a structural-functional correlate

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encinar-et-al-2002-tyrosine-phosphorylation-of-the-inactivating-peptide-of-the-shaker-b-potassium-channel-a-structural.pdf(112.13 KB)
Date
2002-09-12
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Authors
Encinar Hidalgo, José Antonio ; Fernández Carvajal, Asia María ; Molina Gallego, María Luisa ; Molina, A. ; Poveda Larrosa, José Antonio ; Albar, J.P. ; López Barneo, José ; Gavilanes Franco, Francisco ; Ferrer Montiel, Antonio Vicente ; González Ros, José Manuel
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Publisher
American Chemical Society
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Bioquímica y Biología Molecular B e Inmunología
DOI
https://doi.org/10.1021/bi020188u
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info:eu-repo/semantics/article
Description
© 2002 American Chemical Society. This document is the Published version of a Published Work that appeared in final form in Biochemistry. To access the final edited and published work see https://doi.org/10.1021/bi020188u
Abstract
A synthetic peptide patterned after the sequence of the inactivating “ball” domain of the Shaker B K+ channel restores fast (N-type) inactivation in mutant deletion channels lacking their constitutive ball domains, as well as in K+ channels that do not normally inactivate. We now report on the effect of phosphorylation at a single tyrosine in position 8 of the inactivating peptide both on its ability to restore fast channel inactivation in deletion mutant channels and on the conformation adopted by the phosphorylated peptide when challenged by anionic lipid vesicles, a model target mimicking features of the inactivation site in the channel protein. We find that the inactivating peptide phosphorylated at Y8 behaves functionally as well as structurally as the noninactivating mutant carrying the mutation L7E. Moreover, it is observed that the inactivating peptide can be phosphorylated by the Src tyrosine kinase either as a free peptide in solution or when forming part of the membrane-bound protein channel as the constitutive inactivating domain. These findings suggest that tyrosine phosphorylation−dephosphorylation of this inactivating ball domain could be of physiological relevance to rapidly interconvert fast-inactivating channels into delayed rectifiers and vice versa.
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Cell and molecular biology , Genetics , Peptides and proteins , Post-translational modification , Potassium
Citation
Biochemistry, 2002, Vol. 41, N. 40, pp. 12263–12269
URI
http://hdl.handle.net/10201/142861
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