SUMOylation of Myc-family proteins

Arianna Sabò, Mirko Doni, Bruno Amati

Research output: Contribution to journalArticle

Abstract

Myc-family proteins are key controllers of the metabolic and proliferative status of the cell, and are subjected to a complex network of regulatory events that guarantee their efficient and fast modulation by extracellular stimuli. Hence, unbalances in regulatory mechanisms leading to altered Myc levels or activities are often reported in cancer cells. Here we show that c- and N-Myc are conjugated to SUMO proteins at conserved lysines in their C-terminal domain. No obvious effects of SUMOylation were detected on bulk N-Myc stability or activities, including the regulation of transcription, proliferation or apoptosis. N-Myc SUMOylation could be induced by cellular stresses, such as heat shock and proteasome inhibition, and in all instances concerned a small fraction of the N-Myc protein. We surmise that, as shown for other substrates, SUMOylation may be part of a quality-control mechanism acting on misfolded Myc proteins.

Original languageEnglish
Article numbere91072
JournalPLoS One
Volume9
Issue number3
DOIs
Publication statusPublished - Mar 7 2014

Fingerprint

Sumoylation
Small Ubiquitin-Related Modifier Proteins
Proteins
proteins
Complex networks
Proteasome Endopeptidase Complex
Transcription
Quality Control
Lysine
Quality control
Shock
proteasome endopeptidase complex
controllers
Hot Temperature
Cells
Modulation
Apoptosis
quality control
heat stress
lysine

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

SUMOylation of Myc-family proteins. / Sabò, Arianna; Doni, Mirko; Amati, Bruno.

In: PLoS One, Vol. 9, No. 3, e91072, 07.03.2014.

Research output: Contribution to journalArticle

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