title: Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking.
abstract: There are now numerous examples of post-translational modification with geranylgeranyl or farnesyl substituents. Once thought of as solely a mechanism for association of proteins with membranes, other functional aspects of protein prenylation have come to be appreciated. Although, in almost all instances, such proteins are membrane associated, they are often found to also engage in protein-protein interactions. In some instances, such interactions are critical aspects of prenylated protein trafficking. In this review, the role of prenylation in mediating protein-protein interactions will be considered. The hypothesis will be developed that such interactions occur through recognition of the prenyl group and a second domain, on the prenylated protein, by a heterodimeric protein partner.
authors: Department of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Box 70581, Johnson City, TN 37614-0581, USA. sinensky@etsu.edu
authors: M
authors: M
authors: Sinensky
mesh_terms: D000818:Animals; D001665:Binding Sites; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D011106:Polyisoprenyl Phosphates / Q000737:chemistry*; D017368:Protein Prenylation; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013347:Subcellular Fractions / Q000737:chemistry
chemical_list: D008051:Lipid Bilayers; D011106:Polyisoprenyl Phosphates; D011506:Proteins