title: New route for the activation of poly(ADP-ribose) polymerase-1: a passage that links poly(ADP-ribose) polymerase-1 to lipotoxicity?
abstract: In this issue of Biochemical Journal, Chen and colleagues characterize an interaction between ACBD3 (acyl-CoA-binding domain-containing 3) protein and PARP [poly(ADP-ribose) polymerase]-1 through the activation of ERKs (extracellular-signal-regulated kinases). This study envisages a pathway through which ABCD3 translates enhanced fatty acid levels to ERK and consequently PARP-1 activation. The consequences of PARP-1 activation lead to cellular and tissue damage, implying that the ACBD3/PARP-1 pathway is an important pathway in lipotoxicity events.
authors.affiliation: Department of Medical Chemistry, University of Debrecen, Debrecen, H-4032, Hungary MTA-DE Lendület Laboratory of Cellular Metabolism Research Group, Debrecen, H-4032, Hungary Research Center for Molecular Medicine, University of Debrecen, Debrecen, H-4032, Hungary baip@med.unideb.hu.
authors.forename: Péter
authors.initials: P
authors.lastname: Bai
authors.affiliation: Department of Surgery, Rutgers New Jersey Medical School, 185 South Orange Ave, Newark, NJ 07103, U.S.A. Center for Immunity and Inflammation, Rutgers New Jersey Medical School, 185 South Orange Ave, Newark, NJ 07103, U.S.A.
authors.forename: Balázs
authors.initials: B
authors.lastname: Csóka
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000096:biosynthesis*; D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000096:biosynthesis*; D009243:NAD / Q000378:metabolism* / Q000502:physiology*; D011065:Poly(ADP-ribose) Polymerases / Q000096:biosynthesis*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D008565:Membrane Proteins; D009243:NAD; D011065:Poly(ADP-ribose) Polymerases
keywords: ACBD3; ERK; PARP; cholesterol; fatty acid; lipotoxicity