Membrane-associated RING-CH-type finger protein 3 (MARCHF3)

Membrane-associated RING-CH-type finger protein 3 (MARCHF3) is an E3 ubiquitin-protein ligase of the MARCH family, which are distinguished by a RING-CH domain and membrane association[1][2][3][8]. MARCHF3 catalyzes the transfer of ubiquitin from E2 conjugating enzymes to specific substrate proteins, often targeting them for lysosomal or proteasomal degradation[1][2][4][5]. This activity is important for endosomal trafficking and the fine-tuned regulation of cell surface and intracellular proteins, especially in the immune system[1][2][4]. The MARCH family members, including MARCHF3, are emerging as regulators of immune signaling by downregulating immune receptors (such as IL-1 receptor type I), thereby inhibiting inflammatory responses[4]. Dysregulation of MARCHF3 is associated with disorders like cancer (e.g., fibrosarcoma) and leukodystrophy[1]. There are currently no well-documented drugs or biomarkers directly linked to MARCHF3, and its function as a therapeutic target is under investigation, particularly in immunology and oncology[1][4].

Other names

MARCH3RNF173MARCH-IIIE3 ubiquitin-protein ligase MARCHF3RING finger protein 173Membrane-associated RING finger protein 3Membrane-associated RING-CH protein IIIRING-type E3 ubiquitin transferase MARCHF3Membrane-associated ring finger (C3HC4) 3, E3 ubiquitin protein ligase

Ubiquitination of specific target proteins leading to their degradation via the proteasome or lysosome; K48-linked polyubiquitination (canonical degradation signal); Negative regulation of immune signaling by promoting lysosomal degradation of immune receptors (e.g., IL-1 receptor type I)