Mahogunin ring finger protein 1 (MGRN1)

Mahogunin ring finger protein 1 (MGRN1) is a RING-type E3 ubiquitin ligase involved in the post-translational modification of proteins via ubiquitination, tagging substrates for degradation or modulation of cellular localization and function[1][3][4][6]. Highly expressed in neurons, MGRN1 plays a central cytoprotective role by maintaining protein quality control, especially under stress conditions that lead to protein misfolding[1][2]. MGRN1 interacts with chaperones (like Hsp70), is involved in the degradation of misfolded proteins through autophagy and the proteasome, and regulates signaling by G protein-coupled receptors via non-canonical mechanisms[2][3]. Loss of MGRN1 function causes neurodegeneration resembling prion disease in mice, congenital heart defects, and disrupted protein trafficking[1][3][5]. In cellular models, MGRN1 also inhibits the maturation of amyloid precursor protein, implicating it in Alzheimer's pathology[5]. MGRN1 dysfunction has been linked to several human diseases involving protein aggregation and degeneration[4][5][6].

Other names

Mahogunin ring finger-1RNF156KIAA0544E3 ubiquitin-protein ligase MGRN1RING finger protein 156Mahogunin RING finger protein 1RING-type E3 ubiquitin transferase MGRN1

Drugs targeting MGRN1 (none currently established) would likely work by modulating its ubiquitin ligase activity, influencing degradation of specific substrates, protein quality control, or interfering with its regulatory effects on GPCRs or endolysosomal trafficking[1][3][4][5].