Article
Unconventional myristoylation of large-conductance Ca²⁺-activated K⁺ channel (Slo1) via serine/threonine residues regulates channel surface expression.
Proceedings of the National Academy of Sciences of the United States of America - 28 Jun 2011
Alioua Abderrahmane, Li Min, Wu Yong, Stefani Enrico, Toro Ligia
Abstract excerpt
Protein myristoylation is a means by which cells anchor proteins into membranes. The most common type of myristoylation occurs at an N-terminal glycine. However, myristoylation rarely occurs at an internal amino acid residue. Here we tested whether the α-subunit of the human large-conductance voltage- and Ca(2+)-activated K(+) channel (hSlo1) might undergo internal myristoylation. hSlo1 expressed in HEK293T cells...
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