Abstract
The plasmid used to express FLAG-hSnf7N (residues 1-116) in this paper had an unintended missense mutation changing serine at residue 2 to cysteine. We found that this cysteine was palmitoylated. Changing it back to serine decreased the amount of hSnf7N associated with membranes from all for the mutant fragment containing cysteine to approximately half for the wild-type fragment containing serine. The images of FLAG-hSnf7N in Figs. 7B and 8 represent average cells expressing mutant (Cys-2) hSnf7N, whereas for wild-type (Ser-2) hSnf7N, these images correspond to cells expressing high levels of protein. All other plasmids are as indicated, and the conclusions of the paper remain unchanged.
Highlights
Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA؉ ATPase SKD1
The images of FLAG-hSnf7N in Figs. 7B and 8 represent average cells expressing mutant (Cys-2) hSnf7N, whereas for wild-type (Ser-2) hSnf7N, these images correspond to cells expressing high levels of protein
Whitsett PAGE 24501: Fig. 5: An incorrect image was used for the panel A inset
Summary
This paper is available online at www.jbc.org Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA؉ ATPase SKD1. The plasmid used to express FLAG-hSnf7N (residues 1–116) in this paper had an unintended missense mutation changing serine at residue 2 to cysteine.
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