Draft:Regnase-1

Regnase-1 (MCPIP-1, ZC3H12A) is a protien that was first discovered in human peripheral blood monocytes treated the chemotactic protein MCP-1. The protein contains an N-terminal domain, a PilT N-terminus like (PIN) domain, a zinc finger domain, a ubiquitin domain and a C-terminal domain. Two emerging functions of this protein include RNase-cleaving activity (PIN domain) and the control of ubiquitination. Regnase-1 also has implications in cell differentiation, apoptosis, and regulating inflammation.

Regulation of inflammation
NFκB is well known to induce proinflammatory cytokines. Pattern recognition receptors (PRRs) induce NFκB activation via mechanisms that utilize ubiquitylation of RIP1 and TRAF6. Recent studies have shown that Regnase-1 disrupts this ubiquitylation thereby blocking activation of NFκB and its downstream cytokines.