DHHC2 is a proteinS-acyltransferase for Lck

作者：Ruth Zeidman, Gemma Buckland, Marek Cebecauer, Philipp Eissmann, Daniel M. Davis, Anthony I. Magee · 发表于：Molecular Membrane Biology · 年份：2011 · DOI：10.3109/09687688.2011.630682 · 被引用次数：31 · 研究领域：Glycosylation and Glycoproteins Research、Monoclonal and Polyclonal Antibodies Research、Cell Adhesion Molecules Research

Lck is a non-receptor tyrosine kinase of the Src family that is essential for T cell activation. Dual N-terminal acylation of Lck with myristate (N-acylation) and palmitate (S-acylation) is essential for its membrane association and function. Reversible S-acylation of Lck is observed in vivo and may function as a control mechanism. Here we identify the DHHC family protein S-acyltransferase DHHC2 as an enzyme capable of palmitoylating of Lck in T cells. Reducing the DHHC2 level in Jurkat T cells using siRNA causes decreased Lck S-acylation and partial dislocation from membranes, and conversely overexpression of DHHC2 increases S-acylation of an Lck surrogate, LckN10-GFP. DHHC2 localizes primarily to the endoplasmic reticulum and Golgi apparatus suggesting that it is involved in S-acylation of newly-synthesized or recycling Lck involved in T cell signalling.