Akt Kinase Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors

• Published in: The Journal of biological chemistry Vol. 281; no. 6; pp. 3731 - 3737
• Main Authors: Khan, M. Tariq, Wagner, Larry, Yule, David I., Bhanumathy, Cunnigaiper, Joseph, Suresh K.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.02.2006; American Society for Biochemistry and Molecular Biology
• Subjects: Alanine - chemistry; Amino Acid Motifs; Amino Acid Sequence; Animals; Apoptosis; Calcium - metabolism; Calcium Channels - metabolism; Calcium-Transporting ATPases - metabolism; Caspase 3; Caspases - metabolism; Cell Line; Chlorocebus aethiops; CHO Cells; Chromones - pharmacology; COS Cells; Cricetinae; Detergents - pharmacology; DNA, Complementary - metabolism; Enzyme Activation; Glutamic Acid - chemistry; Humans; Immunoprecipitation; Inositol 1,4,5-Trisphosphate Receptors; Microcirculation - metabolism; Molecular Sequence Data; Morpholines - pharmacology; Octoxynol - pharmacology; Phosphatidylinositol 3-Kinases - metabolism; Phosphorylation; Proto-Oncogene Proteins c-akt - metabolism; Receptors, Cytoplasmic and Nuclear - metabolism; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Serine - chemistry; Staurosporine - pharmacology; Time Factors; Transfection

A consensus RXRXX(S/T) substrate motif for Akt kinase is conserved in the C-terminal tail of all three inositol 1,4,5-trisphosphate (IP3) receptor (IP3R) isoforms. We have shown that IP3R can be phosphorylated by Akt kinase in vitro and in vivo. Endogenous IP3Rs in Chinese hamster ovary T-cells were...