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FEBS Lett. 1999 Apr 23;449(2-3):101-4.

Cysteine 29 is the major palmitoylation site on stomatin.

Author information

1
Institute of Biochemistry, University of Vienna, Vienna Biocenter, Austria.

Abstract

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.

PMID:
10338112
DOI:
10.1016/s0014-5793(99)00417-2
[Indexed for MEDLINE]
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