Mutation of Tyrosine in the Conserved NPXXY Sequence Leads to Constitutive Phosphorylation and Internalization, but Not Signaling, of the Human B2 Bradykinin Receptor

• Published in: The Journal of biological chemistry Vol. 279; no. 30; pp. 31268 - 31276
• Main Authors: Kalatskaya, Irina, Schüssler, Steffen, Blaukat, Andree, Müller-Esterl, Werner, Jochum, Marianne, Proud, David, Faussner, Alexander
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 23.07.2004
• Subjects: Amino Acid Sequence; Cell Line; Conserved Sequence; GTP-Binding Protein alpha Subunits, Gq-G11 - metabolism; Humans; In Vitro Techniques; Kinetics; Ligands; Mutagenesis, Site-Directed; Phosphorylation; Protein Conformation; Receptor, Bradykinin B2 - chemistry; Receptor, Bradykinin B2 - genetics; Receptor, Bradykinin B2 - metabolism; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Signal Transduction; Tyrosine - chemistry; Tyrosine - genetics

Although the G protein-coupled receptors (GPCRs) share a similar seven-transmembrane domain structure, only a limited number of amino acid residues is conserved in their protein sequences. One of the most highly conserved sequences is the NP XX Y motif located at the cytosolic end of the transmembra...