Sleeman J P, Rahmsdorf U, Steffen A, Ponta H, Herrlich P
Forschungszentrum Karlsruhe, Institute of Genetics, Germany.
Eur J Biochem. 1998 Jul 1;255(1):74-80. doi: 10.1046/j.1432-1327.1998.2550074.x.
Functional differences between members of the CD44 family of cell surface glycoproteins is mediated in part by differential post-translational modification of these proteins and by alternative splicing. Tyrosine sulphation is a secondary modification of the primary amino acid structure of a number of secreted, transmembrane and lysosomal proteins, which is associated with promotion of protein-protein interactions. Here we identify a cannonical tyrosine-sulphation motif within rat and mouse CD44 exon v5. We show that inorganic sulphate is incorporated into the metastasis-associated rat CD44v4-v7 splice variant. The sulphate is not incorporated into sulphated glycosaminoglycan or other sugar modifications of CD44v4-v7. A point mutation of the exon v5 tyrosine to phenylalanine destroys inorganic sulphate incorporation into CD44v4-v7. These results demonstrate that the tyrosine-sulphation motif within rat CD44 exon v5 is used in vivo, and suggest that exon v5 may be involved in mediating CD44 ligand binding-activity by means of its sulphated tyrosine.
