Midnolin (MIDN)

Midnolin (MIDN) is a nuclear adaptor protein containing three conserved domains: an N-terminal ubiquitin-like domain, a central “Catch” domain that binds substrate degrons, and a C-terminal α helix that associates with the proteasome[1][2][3][4]. MIDN promotes selective degradation of a broad set of nuclear proteins—especially transcription factors encoded by immediate-early genes—through a ubiquitin-independent proteasomal pathway[1][2][3][4]. It plays regulatory roles in metabolic signaling in pancreatic beta cells and is crucial for neuronal development, with loss of MIDN linked to impaired neurite outgrowth and increased risk for sporadic Parkinson's disease[3]. Recent evidence also connects MIDN to oncogenic progression in B-cell malignancies: MIDN augments proteasome activity and enhances survival and proliferation of these cancer cells[1]. MIDN is not a traditional drug target such as a receptor or enzyme; there are no approved drugs known to specifically modulate its function at present[3].

Other names

MidnolinMIDNStxMidbrain nucleolar proteinstuxnet homolog (Drosophila)midbrain nucleolar proteinstuxnet homolog