ATP-binding cassette sub-family E member 1 (ABCE1)

ATP-binding cassette sub-family E member 1 (ABCE1) is a highly conserved, essential ATPase enzyme in the ATP-binding cassette superfamily, specifically the OABP subfamily[1][3][2]. Uniquely among ABC proteins, ABCE1 is soluble (not membrane-bound) and contains two C-terminal ABC domains and an N-terminal cysteine-rich domain that coordinates iron-sulfur ([4Fe-4S]) clusters crucial for its activity[1][2]. ABCE1 functions mainly as a ribosome recycling factor during translation termination, helping to dissociate ribosomes for subsequent rounds of protein synthesis[2][4]. In addition, ABCE1 inhibits the antiviral ribonuclease L pathway by directly binding and suppressing RNase L, thus controlling interferon-regulated antiviral activity[1][3]. It plays further roles in mRNA surveillance, protein quality control, and is implicated in cancer cell proliferation and antiapoptotic pathways[1][3][2]. Mutations or dysregulation of ABCE1 are associated with diseases including prostate cancer and certain viral infections. No small-molecule therapeutics directly target ABCE1 as of current knowledge, and systemic inhibition would be highly problematic due to its essential cellular functions[3][1].

Other names

ABCE1ABC38OABPRLIRNASEL1RNASELIRNS4IRLI12'-5'-oligoadenylate-binding proteinHuHP68RNase L inhibitorRibonuclease 4 inhibitorRNase L inhibitor 1ATP-binding cassette subfamily E member 1ribonuclease 4 inhibitorribonuclease L (2',5'-oligoisoadenylate synthetase-dependent) inhibitorribonuclease L inhibitor 1

Inhibition of ABCE1 would release its suppression of RNase L, potentially enhancing antiviral responses[3]. Targeting ABCE1 could modulate ribosome recycling and translation control but is not an established mechanism for approved drugs[3].