van't Hof Wouter, Crystal Ronald G
Institute of Genetic Medicine, Weill Medical College of Cornell University, New York, New York 10021, USA.
J Virol. 2002 Jun;76(12):6382-6. doi: 10.1128/jvi.76.12.6382-6386.2002.
Membrane-proximal cysteines 259 and 260 in the cytoplasmic tail of the coxsackievirus and adenovirus receptor (CAR) are known to be essential for the tumor suppression activity of CAR. We demonstrate that these residues provide an S-acylation motif for modification of CAR with the fatty acid palmitate. Substitution of alanine for cysteines 259 and 260 results in the additional localization of CAR in perinuclear compartments with no effect on the efficiency of adenovirus infection. The results indicate that palmitylation is important for stable plasma membrane expression and biological activity of CAR but is not critical for adenovirus receptor performance.
柯萨奇病毒和腺病毒受体（CAR）胞质尾中的膜近端半胱氨酸259和260已知对CAR的肿瘤抑制活性至关重要。我们证明这些残基为CAR与脂肪酸棕榈酸酯的修饰提供了一个S-酰化基序。用丙氨酸取代半胱氨酸259和260会导致CAR在核周区室中额外定位，而对腺病毒感染效率没有影响。结果表明，棕榈酰化对于CAR在质膜上的稳定表达和生物学活性很重要，但对腺病毒受体功能并不关键。
