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rAMPing Up Stress Signaling: Protein AMPylation in Metazoans

Matthias C Truttmann1, Hidde L Ploegh2

  • 1Boston Children's Hospital, Boston, MA, USA.

Trends in Cell Biology
|April 24, 2017
PubMed

Insights

Protein AMPylation, a post-translational modification, involves adding AMP to proteins. This process, mediated by fic-domain enzymes, impacts cell signaling, stress response, and proteostasis in metazoans, and is exploited by pathogens.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Protein AMPylation is a post-translational modification (PTM) involving the covalent attachment of AMP to amino acid residues.
  • This modification utilizes ATP as the AMP donor and is catalyzed by fic-domain-containing AMPylases.
  • AMPylation plays a crucial role in both normal and pathological cellular signaling pathways.

Purpose of the Study:

  • To review the endogenous and parasitic protein AMPylation in metazoans.
  • To summarize the current understanding of how fic-domain-containing AMPylases regulate cellular proteostasis.
  • To highlight the role of AMPylation in cell signaling and stress response.

Main Methods:

  • Literature review of existing research on protein AMPylation.
  • Analysis of the function of fic-domain-containing AMPylases in metazoans.
  • Investigation of bacterial exploitation of host AMPylation pathways.

Main Results:

  • Fic-domain AMPylases in metazoans modify specific protein targets, influencing cellular stress perception and regulation.
  • Pathogenic bacteria can hijack host AMPylation machinery to manipulate host cell signaling for their own benefit.
  • AMPylation is integral to maintaining cellular proteostasis.

Conclusions:

  • Protein AMPylation is a significant PTM with broad implications in cellular regulation and disease.
  • Fic-domain AMPylases are key regulators of cellular processes, including stress response and proteostasis.
  • Understanding AMPylation mechanisms is crucial for deciphering host-pathogen interactions and developing therapeutic strategies.
Keywords:
Grp78/BiPadenylylationendoplasmic reticulumheat shock proteinprotein aggregation

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