Institut für Humangenetik, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany.
FEBS Lett. 2011 Sep 2;585(17):2665-70. doi: 10.1016/j.febslet.2011.07.028. Epub 2011 Jul 31.
Many G-protein coupled receptors are palmitoylated in their C-terminal, intracellular regions. So far no enzymes responsible for this modification have been described. We identified an interaction of the membrane proximal helix 8 of somatostatin receptor 5 (SSTR5) with the N-terminal region of the putative palmitoyltransferase ZDHHC5 using the Ras recruitment interaction screening system. ZDHHC5 and SSTR5 are colocalized at the plasma membrane and can be efficiently coimmunoprecipitated from transfected cells. Coexpression of ZDHHC5 in HEK293 cells increased palmitoylation of SSTR5 whereas knock-down of endogenous ZDHHC5 by siRNAs decreased it. Our data identify the first palmitoyltransferase for a G-protein coupled receptor.
许多 G 蛋白偶联受体在其 C 端胞内区域发生棕榈酰化。到目前为止，尚未描述负责这种修饰的酶。我们使用 Ras 募集相互作用筛选系统鉴定了生长抑素受体 5（SSTR5）的膜近端螺旋 8 与假定的棕榈酰转移酶 ZDHHC5 的 N 端区域之间的相互作用。ZDHHC5 和 SSTR5 在质膜上共定位，并且可以从转染的细胞中有效地共免疫沉淀。ZDHHC5 在 HEK293 细胞中的共表达增加了 SSTR5 的棕榈酰化，而 siRNA 对内源性 ZDHHC5 的敲低则降低了棕榈酰化。我们的数据确定了第一个 G 蛋白偶联受体的棕榈酰转移酶。
