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The simplest interpretation of these results is that small increases in both E2 14k and E3alpha in muscles of insulin-deficient animals together accelerate Ub conjugation and protein degradation by the N-end rule pathway, the same pathway activated in cancer cachexia, sepsis, and hyperthyroidism.
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The N-end rule relates the regulation of the in vivo half-life of a protein to the identity of its N-terminal residue.
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Lecker, S. Because recent studies have suggested that this increased proteolysis is due to activation of the ubiquitin-proteasome Ub-proteasome pathway, we investigated whether diabetes is associated with an increased rate of Ub conjugation to muscle protein. This enhanced Ub-conjugation occurred mainly through the N-end rule pathway that involves E2 14k and E3alpha.
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