Fatty acid modification of the coxsackievirus and adenovirus receptor

Wouter Van't Hof, Ronald Crystal

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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.

Original languageEnglish
Pages (from-to)6382-6386
Number of pages5
JournalJournal of Virology
Issue number12
Publication statusPublished - 5 Jun 2002
Externally publishedYes


ASJC Scopus subject areas

  • Immunology

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