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SUMOylation of Myc-family proteins.

PloS one (2014-03-13)
Arianna Sabò, Mirko Doni, Bruno Amati
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.

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Sigma-Aldrich
Anti-vinculina monoclonale, clone hVIN-1, purified from hybridoma cell culture
Sigma-Aldrich
Anti-N-Myc Mouse mAb (NCM II 100), liquid, clone NCM II 100, Calbiochem®
Sigma-Aldrich
Anti-SUMO-1 antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution