Cysteine 29 is the major palmitoylation site on stomatin

FEBS Letters

Umlauf, Ellen¹  Prohaska, Rainer¹  Snyers, Luc¹ 

[1] Institute of Biochemistry, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria

关键词: Membrane protein;    Amniotic cell;    Microvillus;   

DOI  :  10.1016/S0014-5793(99)00417-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown