Membrane-associated ring-CH-type finger protein 10 (MARCHF10)

Membrane-associated ring-CH-type finger protein 10 (MARCHF10) is a member of the MARCH family of membrane-bound E3 ubiquitin ligases. These enzymes catalyze the transfer of ubiquitin to lysine residues of substrate proteins, often targeting them for proteasomal degradation or affecting their membrane localization and stability. MARCHF10 is predicted to contain a RING-CH domain (a variant of the canonical RING finger domain) and likely binds zinc ions as part of its structural motif. MARCH family proteins, including MARCHF10, act as critical regulators of immune responses by targeting immune receptors, viral proteins, and other membrane proteins for ubiquitination, thereby modulating their expression or activity at the cell surface. This regulation is relevant to processes such as immune surveillance, inflammation, and cellular homeostasis. Dysregulation of MARCH family ligases has been implicated in cancer, metabolic diseases, immune disorders, and primary ciliary dyskinesia. Although the biological context of MARCHF10's direct therapeutic targeting remains under investigation, E3 ubiquitin ligases are emerging as important drug targets because of their key regulatory roles in health and disease. No specific therapeutic drugs or biomarkers have yet been established for MARCHF10, but safety concerns for this family include risks of immune perturbation and off-target protein degradation due to broad substrate specificity.

Other names

Membrane-associated ring-CH-type finger 10MARCH10RNF190MARCH-XFLJ35757Membrane-associated RING finger protein 10Membrane-associated RING-CH protein XRing finger protein 190RING-type E3 ubiquitin transferase MARCHF10Testis secretory sperm-binding protein Li 228nEC 2.3.2.27

Ubiquitination of substrate proteins, Targeted proteasomal degradation, Posttranslational modification of membrane or signaling proteins