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misfolded TDP-43 (show TARDBP Proteins) is cleared by VHL (show VHL Proteins)/CUL2 in a step-wise manner via fragmentation.
Cullins are a family of NEDD8 (show NEDD8 Proteins) targets important in the stabilization and degradation of proteins, such as hypoxia-inducible factor (HIF1A (show HIF1A Proteins)), via Cullin-2.
Nevertheless, the identification of the Cul2 box may allow prediction of Cullin specificity for all E4orf6-containing Adenoviridae.
a novel link between the oncoprotein PRAME and the conserved EKC complex
Study finds that UBXN7 over-expression converts CUL2 to its neddylated form and causes the accumulation of non-ubiquitylated HIF1alpha (show HIF1A Proteins).
The authors applied protein-complex purification strategies and identified PRAME (show PRAME Proteins) as a substrate recognition subunit of a Cullin2-based E3 ubiquitin ligase (show MUL1 Proteins).
The data suggest that neither HIF1alpha (show HIF1A Proteins) nor CUL2 mutation may play a central role in HIF1alpha (show HIF1A Proteins) activation in gastric, colorectal, breast, lung and hepatocellular carcinomas, and acute leukemias.
Cullin selection is determined by specific Elongin C (show TCEB1 Proteins) and Skp1 (show SKP1 Proteins) sequences
the HPV16 E7-associated cullin 2 ubiquitin ligase complex contributes to aberrant degradation of the pRB (show RB1 Proteins) tumor suppressor in HPV16 E7-expressing cells.
CUL2 is required for normal vasculogenesis, at least in part mediated by its regulation of HIF-mediated transcription.
Authors show that bovine immunodeficiency virus Vif (show BTG1 Proteins) interacts with Cullin 2 (CUL2), ELOB (show TCEB2 Proteins)/C, and RBX1 (show RBX1 Proteins), but not with CBF-beta (show CBFB Proteins) or CUL5 (show CUL5 Proteins), to form a CRL2 (show DAND5 Proteins) E3 ubiquitin ligase (show MUL1 Proteins) and degrade the restrictive bovine APOBEC3 (show APOBEC3F Proteins) proteins (A3Z2Z3 and A3Z3 (show APOBEC3F Proteins)).
CUL-2 RING E3 ubiquitin-ligase (show MUL1 Proteins) acts at multiple levels to control germline development; CUL-2 may similarly regulate germline development in other organisms as well.
Results indicate that LRR-1 (show LRR1 Proteins) acts as a nuclear substrate-recognition subunit of a Cullin 2-RING E3 ligase complex (CRL2 (show DAND5 Proteins)(LRR-1 (show LRR1 Proteins))), which ensures DNA replication integrity.
The C. elegans p97/CDC-48 (show vcp Proteins)-UFD-1 (show UFD1L Proteins)-NPL-4 complex controls the sperm-oocyte switch by regulating CUL-2-mediated TRA-1A proteasome degradation.
segregation of the germ plasm involves both stabilization of germline proteins in the germ line and cullin-dependent degradation in the soma
Results establish that zyg-11 and the cullin cul-2 promote the metaphase-to-anaphase transition and M phase exit at meiosis II in Caenorhabditis elegans.
Data show that inactivation of ZYG-11 produces meiotic and polarity reversal defects similar to those observed in CUL-2 mutants, suggesting that the two proteins function in the same pathways.
oocyte maturation from pachytene exit and MPK-1 (show MAPK1 Proteins) activation are redundantly controlled by the RBX-2-CUL-5 (show CUL5 Proteins)- and RBX-1 (show RBX1 Proteins)-CUL-2-based complexes.
TRA-1 is regulated by degradation mediated by a CUL-2-based ubiquitin ligase complex
Fem-1 protein is a substrate-specific adaptor for a CUL-2-based ubiquitin ligase.
MEL-26 levels are kept low by the action of another type of ubiquitin ligase, which contains CUL-2
Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF).
, cullin-2 (cul-2)
, cullin 2