Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family

• DOI: 10.1073/pnas.1017082108
• Publication Date: 2011-09-13T06:44:44Z
• Authors: Sung Hoon Cho; Annie K. Ahn; Prerna Bhargava; Chih-Hao Lee; Christine M. Eischen; Owen McGuinness; Mark Boothby
• Keywords: Male; Mice, Knockout; 0301 basic medicine; B-Lymphocytes; Mice, 129 Strain; Lymphoma; Immunoblotting; Apoptosis; Biological Transport; AMP-Activated Protein Kinases; Mitochondria; Enzyme Activation; Mice, Inbred C57BL; Mice; 03 medical and health sciences; Glucose; In Situ Nick-End Labeling; Animals; Female; Interleukin-4; Glycolysis; Cells, Cultured

Poly(ADP-ribose)polymerase (PARP)14—a member of the B aggressive lymphoma (BAL) family macrodomain-containing PARPs—is an ADP ribosyltransferase that interacts with Stat6, enhances induction certain genes by IL-4, and is expressed in lymphocytes. We now show IL-4 enhancement glycolysis cells requires PARP14 this process central to a role IL-4–induced survival. Thus, enhancements AMP-activated protein kinase activity restored both glycolytic Parp14 −/− prosurvival signaling cytokine. Suppression apoptosis B-lymphoid oncogenesis, elevated macro-PARP expression has been correlated aggressiveness. Strikingly, deficiency delayed lymphomagenesis reversed block B-cell maturation driven Myc oncogene. Collectively, these findings reveal links between mammalian ribosyltransferase, cytokine-regulated metabolic activity, apoptosis; influences Myc-induced oncogenesis; suggest PARP14-dependent capacity increase cellular rates may be important determinant pathobiology.