Fatty acid modification of the coxsackievirus and adenovirus receptor.
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.
van't Hof
Wouter
W
Institute of Genetic Medicine, Weill Medical College of Cornell University, New York, New York 10021, USA. geneticmedicine@med.cornell.edu
Crystal
Ronald G
RG
D000215:Acylation; D000256:Adenoviridae / Q000235:genetics / Q000502:physiology; D000818:Animals; D001980:Bronchi / Q000166:cytology; D016466:CHO Cells; D019556:COS Cells; D002478:Cells, Cultured; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D006224:Cricetinae; D004847:Epithelial Cells; D005786:Gene Expression Regulation; D005822:Genetic Vectors; D006801:Humans; D010168:Palmitates / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
C568771:CLMP protein, human; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D010168:Palmitates; D011991:Receptors, Virus