E3 ubiquitin-protein ligase MARCHF2 (MARCHF2)

E3 ubiquitin-protein ligase MARCHF2 (MARCHF2) is a membrane-associated E3 ubiquitin ligase that catalyzes the transfer of ubiquitin from an E2 enzyme to selected lysine residues on target proteins, thereby tagging them for endocytosis, lysosomal degradation, or altered trafficking. MARCHF2 modulates surface availability and degradation of several glycoproteins, such as TFRC (transferrin receptor) and CD86, and participates in vesicular transport processes involving the endosome and trans-Golgi network. It regulates protein trafficking and secretion, negatively modulates the antiviral and antibacterial immune response through suppression of NF-κB and type 1 interferon pathways (by promoting proteasomal degradation of NEMO/IKBKG), and plays a role in controlling the immune cell surface proteome. Genetic or functional disruption of MARCHF2 can contribute to immune-related diseases and has been linked to rare disorders such as Immunodeficiency 33 and pulmonary aspergilloma[1][2][3][7].

Other names

Membrane-associated ring-CH-type finger 2MARCH2MARCH-IIRNF172HSPC240Membrane-associated ring finger protein 2Membrane-associated ring finger (C3HC4) 2, E3 ubiquitin protein ligaseRING-type E3 ubiquitin transferase MARCHF2

Drugs would likely act as inhibitors or modulators of E3 ubiquitin ligase activity, affecting ubiquitination of specific substrate proteins and thus protein turnover, membrane receptor expression, or immune signaling.