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Cysteine 29 is the major palmitoylation site on stomatin
Author(s) -
Snyers Luc,
Umlauf Ellen,
Prohaska Rainer
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00417-2
Subject(s) - palmitoylation , biochemistry , cysteine , chemistry , palmitic acid , serine , immunoprecipitation , hek 293 cells , membrane protein , membrane , fatty acid , phosphorylation , enzyme , gene
The 31 kDa membrane protein stomatin was metabolically labeled with tritiated palmitic acid in the human amniotic cell line UAC and immunoprecipitated. We show that the incorporated palmitate is sensitive to hydroxylamine, indicating the binding to cysteine residues. Stomatin contains three cysteines. By expressing a myc‐tagged stomatin and substituting the three cysteines by serine, individually or in combination, we demonstrate that Cys‐29 is the predominant site of palmitoylation and that Cys‐86 accounts for the remaining palmitate labeling. Disruption of Cys‐52 alone does not show any detectable reduction of palmitic acid incorporation. Given the organization of stomatin into homo‐oligomers, the presence of multiple palmitate chains is likely to increase greatly the affinity of these oligomers for the membrane and perhaps particular lipid domains within it.