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NIH Research Festival

September 14 – 16, 2016

Role of TRIM72 ADP-ribosylation cycle in myocardial injury and membrane repair

Thursday, September 15, 2016 – Poster Session II
12:00 – 1:30 p.m.

FAES Terrace

NHLBI

CELLBIO-5

Authors

  • H Ishiwata-Endo
  • J Kato
  • A Tonouchi
  • YW Chung
  • J Sun
  • LA Stevens
  • J Zhu
  • AM Aponte
  • DA Springer
  • H San
  • K Takeda
  • ZX Yu
  • V Hoffmann
  • E Murphy
  • J Moss

Abstract

Specific mono-ADP-ribosylation of a protein arginine catalyzed by ADP-ribosyltransferase 1 (ART1), i.e., transfer of ADP-ribose from NAD to acceptor arginine, is reversed by ADP-ribosylarginine hydrolase 1 (ARH1) cleavage of the ADP-ribose-arginine bond. ARH1-deficient mice developed gender-specific cardiomyopathy, with myocardial fibrosis, impaired myocardial function, and ischemia-reperfusion injury. Membrane-repair protein TRIM72 was identified as substrate for ART1 and ARH1; ADP-ribosylated TRIM72 levels were greater in ARH1-deficient mice following ischemia-reperfusion injury. In C2C12 myocytes, ARH1 knockdown increased ADP-ribosylation of TRIM72, and delayed wound healing. Mutant TRIM72(R207K, R260K) that is not ADP-ribosylated, interfered with assembly of TRIM72 repair complexes at site of laser-induced injury. We hypothesized that regulatory enzymes ART1 and ARH1 and substrate TRIM72 would be in complexes and, were co-immunoprecipitated from mouse heart lysates. We propose a mono-ADP-ribosylation cycle involving recruitment of TRIM72 and other required molecules to sites of membrane damage is critical for wound repair and healing following myocardial injury.

Scientific Focus Area: Cell Biology

This page was last updated on Friday, March 26, 2021

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