Membrane-associated RING-CH-type finger protein 11 (MARCHF11)

Membrane-associated RING-CH-type finger protein 11 (MARCHF11) is a member of the MARCH family of E3 ubiquitin ligases characterized by a RING-CH-type zinc finger domain anchored to cellular membranes. As an E3 ubiquitin ligase, MARCHF11 mediates the transfer of ubiquitin from an E2 conjugating enzyme onto substrate proteins, thereby signaling processes such as their degradation, sorting, or altered intracellular trafficking. MARCHF11 appears to have a role in ubiquitin-dependent protein sorting in the trans-Golgi network and multivesicular body pathway, and has been identified to mediate polyubiquitination of CD4, potentially regulating cell surface protein expression. Like other MARCH family members, it may contribute to the regulation of immune responses and other cell signaling processes, though specific disease associations and pharmacological modulators targeting this protein have not been established.

Other names

E3 ubiquitin-protein ligase MARCHF11MARCH11MARCH-XIRNF226Membrane-associated RING finger protein 11Membrane-associated RING-CH protein XIRING-type E3 ubiquitin transferase MARCHF11Ring finger protein 226

Polyubiquitination of substrate proteins (e.g., CD4) leading to altered cellular localization, signaling, or degradation