"We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex."

"Moreover, expression of ASB11 can increase Ribophorin 1 protein turnover in vivo."

"Here, we identify Cul5-ASB11 as the E3 ligase targeting BIK for ubiquitination and degradation."

"These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex."

"We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig."

"As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig."

"These findings support that ER stress–induced and ASB11-mediated BIK degradation plays a pro-survival role to contribute to the adaptive phase of UPR."

"Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase."

"UBE2F, a neddylation E2, neddylates CUL5 to activate cullin-RING ligase-5, upon coupling with neddylation E3 RBX2/SAG."

"Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."

"The polyubiquitinated PAICS recruits ubiquitin-associated protein 2 (UBAP2), a ubiquitin-binding protein with multiple stretches of intrinsically disordered regions, thereby inducing phase separation to trigger purinosome assembly for enhancing DNPS pathway flux."

"Hypoxia impairs factor-inhibiting hypoxia-1 (FIH)-dependent ASB11 hydroxylation, promoting ASB11-mediated ERLIN1 degradation."

"MS fragmentation studies provided evidence that ASB11 and P18-INK4C proteins undergo both monohydroxylation and dihydroxylation reactions within their VNVN motif (Figs 3, S14 and S15)."

"Consistent with these results, d-Asb11 was able to specifically ubiquitylate and degrade DeltaA both in vitro and in vivo."

"These results showed that the Cul5 box of d-Asb11 is essential for its function to activate the Notch target gene hes1 through Notch pathway."

"We conclude that d-Asb11 is a novel regulator of the neuronal progenitor compartment size by maintaining the neural precursors in the proliferating undifferentiated state possibly through the control of SoxB1 transcription factors."

"Thus, the expression of d-asb11 is necessary for muscle progenitor expansion, whereas its downregulation marks the onset of terminal differentiation."