Fig. 6: DPEP2 is degraded by Trim32-mediated ubiquitination modification in activated macrophages.
From: The Trim32-DPEP2 axis is an inflammatory switch in macrophages during intestinal inflammation
A MG132 treatment but not CHX inhibited the downregulation of DPEP2 in LPS-treated macrophages. B LPS treatment induces increased DPEP2 ubiquitination in macrophages. C Knockdown of Trim32 but not Rmnd5a, Egr2, Dtx2, Ufl2, Smurf2, Herc4, Ube2i, Ubr5 or Znf598 repress the DPEP2 ubiquitination in activated macrophages. D More interaction of DPEP2 and Trim32 protein was detected in the activated pro-inflammatory macrophages. E Pattern diagram of Trim32-WT, Trim32-ΔRING, Trim32 C21S and Trim32 C39S protein. F Trim32-ΔRING decreases the ubiquitination of DPEP2 and stabilizes DPEP2 proteins responding to inflammatory stimulation in macrophages. RING-deficient Trim32, Trim32 C21S (G) or Trim32 C39S (H), downregulated both ubiquitination and degradation of DPEP2. Repression the catalytic activity of Trim32 as an E3 ubiquitin-protein ligase has no influence on the mRNA levels of DPEP2 in iBMDMs (I) and THP-1 (J). All data are expressed as mean ± SD. ns denotes no signification.
