The Protein Scaffold NHERF-1 Controls the Amplitude and Duration of Localized Protein Kinase D Activity

• Published in: The Journal of biological chemistry Vol. 284; no. 36; pp. 24653 - 24661
• Main Authors: Kunkel, Maya T., Garcia, Erin L., Kajimoto, Taketoshi, Hall, Randy A., Newton, Alexandra C.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04.09.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Motifs - physiology; Animals; Carcinogens - pharmacology; Cell Membrane - genetics; Cell Membrane - metabolism; Cytosol - metabolism; Dogs; Fluorescence Resonance Energy Transfer; HeLa Cells; Humans; Isoenzymes - genetics; Isoenzymes - metabolism; Mechanisms of Signal Transduction; Phorbol Esters - pharmacology; Phosphoproteins - genetics; Phosphoproteins - metabolism; Protein Kinase C - genetics; Protein Kinase C - metabolism; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Structure, Tertiary - physiology; Protein Transport - drug effects; Protein Transport - physiology; Signal Transduction - drug effects; Signal Transduction - physiology; Sodium-Hydrogen Exchangers - genetics; Sodium-Hydrogen Exchangers - metabolism

Protein kinase D (PKD) transduces an abundance of signals downstream of diacylglycerol production. The mammalian PKD family consists of three isoforms, PKD1, PKD2, and PKD3; of these PKD1 and PKD2 contain PDZ-binding motifs at their carboxyl termini. Here we show that membrane-localized NHERF scaffo...