Elizabeth Petro - Diacylglycerol kinase θ: Regulation and stability

Document created by Elizabeth Petro on Aug 22, 2014
Version 1Show Document
  • View in full screen mode

  Publication Details (including relevant citation   information):

  Tu-Sekine, Becky, Goldschmidt, Hana, Petro, Elizabeth, Raben,   Daniel M., Advances in Biological Regulation 2013   Jan;53(1):118-26. doi: 10.1016/j.jbior.2012.09.007. Epub 2012 Sep   20.


  Given the well-established roles of diacylglycerol (DAG) and   phosphatidic acid (PtdOH) in a variety of signaling cascades, it   is not surprising that there is an increasing interest in   understanding their physiological roles and mechanisms that   regulate their cellular levels. One class of enzymes capable of   coordinately regulating the levels of these two lipids is the   diacylglycerol kinases (DGKs). These enzymes catalyze the   transfer of the γ-phosphate of ATP to the hydroxyl group of DAG,   which generates PtdOH while reducing DAG. As these enzymes   reciprocally modulate the relative levels of these two signaling   lipids, it is essential to understand the regulation and roles of   these enzymes in various tissues. One system where these enzymes   play important roles is the nervous system. Of the ten mammalian   DGKs, eight of them are readily detected in the mammalian central   nervous system (CNS): DGK-α, DGK-β, DGK-γ, DGK-η, DGK-ζ, DGK-ι,   DGK-ε, and DGK-θ. Despite the increasing interest in DGKs, little   is known about their regulation. We have focused some attention   on understanding the enzymology and regulation of one of these   DGK isoforms, DGK-θ. We recently showed that DGK-θ is regulated   by an accessory protein containing polybasic regions. We now   report that this accessory protein is required for the previously   reported broadening of the pH profile observed in cell lysates in   response to phosphatidylserine (PtdSer). Our data further reveal   DGK-θ is regulated by magnesium and zinc, and sensitive to the   known DGK inhibitor R599022. These data outline new parameters   involved in regulating DGK-θ.

  Address (URL): http://www.sciencedirect.com/science/article/pii/S2212492612000917