New route for the activation of poly(ADP-ribose) polymerase-1: a passage that links poly(ADP-ribose) polymerase-1 to lipotoxicity?

Péter Bai; Balázs Csóka

doi:10.1042/BJ20150598

New route for the activation of poly(ADP-ribose) polymerase-1: a passage that links poly(ADP-ribose) polymerase-1 to lipotoxicity?

Biochem J. 2015 Jul 15;469(2):e9-11. doi: 10.1042/BJ20150598.

Authors

Péter Bai¹, Balázs Csóka²

Affiliations

¹ 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.
² 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.

PMID: 26171833
DOI: 10.1042/BJ20150598

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.

Keywords: ACBD3; ERK; PARP; cholesterol; fatty acid; lipotoxicity.

Publication types

Comment

MeSH terms

Adaptor Proteins, Signal Transducing / biosynthesis*
Animals
Humans
Membrane Proteins / biosynthesis*
NAD / metabolism*
NAD / physiology*
Poly(ADP-ribose) Polymerases / biosynthesis*

Substances

Adaptor Proteins, Signal Transducing
Membrane Proteins
NAD
Poly(ADP-ribose) Polymerases