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. Author manuscript; available in PMC: 2015 Sep 1.
Published in final edited form as: Trends Cell Biol. 2014 May 24;24(9):546–553. doi: 10.1016/j.tcb.2014.04.008

Figure 2.

Figure 2

Models for how ubiquitination can affect Ago proteins. (Top) Unloaded Ago proteins in many cellular contexts are susceptible to degradation by ubiquitin-proteasome and/or autophagosome-dependent pathways. These mechanisms adjust the level of Ago proteins in concert with miRNA biogenesis. (Bottom) During T cell activation, the ubiquitination-dependent turnover of Ago2 is associated with overall downregulation of miRNA accumulation. This may facilitate the re-setting of a different miRNA repertoire in activated T cells, in which the “old” miRNA/Ago pool is actively degraded and replaced with newly transcribed miRNAs and newly synthesized Ago proteins.