Ubiquitin-conjugating enzyme E2 Q-like protein 1 (UBE2QL1)

Ubiquitin-conjugating enzyme E2 Q-like protein 1 (UBE2QL1) is an E2 ubiquitin-conjugating enzyme that plays a central role in the ubiquitination of proteins on damaged lysosomal membranes, a process essential for lysophagy—the selective autophagic clearance of damaged lysosomes[1][2]. Upon lysosomal damage, UBE2QL1 rapidly translocates to damaged lysosomes, facilitating the formation of K48-linked ubiquitin chains that coordinate the recruitment of autophagy effectors, notably p62 and VCP/p97[1][2]. Depletion of UBE2QL1 impairs lysophagy, reduces cell survival after lysosomal damage, and disrupts lysosomal homeostasis even under unstressed conditions. UBE2QL1 is thus essential for both acute lysosomal damage responses and the baseline maintenance of lysosomal integrity, implicating it in cellular homeostasis and possible roles in degenerative diseases[1][2][3]. Key findings indicate that UBE2QL1 has functional specialization within its enzyme family, lacks domains present in other UBE2Q members, and may be indispensable in some cell types[1]. While the enzyme is not currently directly targeted by therapeutic drugs and no clinically used inhibitors or biomarkers exist, its essential roles in protein quality control and lysosome integrity highlight it as biologically significant and a potential therapeutic target for relevant pathologies[1][2][3].

Other names

UBE2QL1FLJ25076E2Q-like ubiquitin-conjugating enzyme 1ubiquitin-conjugating enzyme E2Q-like protein 1ubiquitin conjugating enzyme E2 Q family like 1ubiquitin-conjugating enzyme E2Q family-like 1