scholarly journals Notch Signaling Is Antagonized by SAO-1, a Novel GYF-Domain Protein That Interacts with the E3 Ubiquitin Ligase SEL-10 in Caenorhabditis elegans

Genetics ◽  
2011 ◽  
Vol 190 (3) ◽  
pp. 1043-1057 ◽  
Author(s):  
Valerie A. Hale ◽  
Evan L. Guiney ◽  
Lindsey Y. Goldberg ◽  
Josephine H. Haduong ◽  
Callie S. Kwartler ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Notch Signaling ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Domain Protein

scholarly journals In Vitro Enhanced Sensitivity to Cisplatin in D67Y BRCA1 RING Domain Protein

2011 ◽  
Vol 5 ◽  
pp. BCBCR.S8184 ◽  
Author(s):  
Apichart Atipairin ◽  
Adisorn Ratanaphan
Keyword(s):  
Dna Damage ◽  
Ubiquitin Ligase ◽  
Dna Damage Repair ◽  
E3 Ubiquitin Ligase ◽  
Chemotherapeutic Agents ◽  
Ring Domain ◽  
Protein Ubiquitination ◽  
Damage Repair ◽  
Domain Protein

BRCA1 is a tumor suppressor protein involved in maintaining genomic integrity through multiple functions in DNA damage repair, transcriptional regulation, cell cycle checkpoint, and protein ubiquitination. The BRCA1-BARD1 RING complex has an E3 ubiquitin ligase function that plays essential roles in response to DNA damage repair. BRCA1-associated cancers have been shown to confer a hypersensitivity to chemotherapeutic agents. Here, we have studied the functional consequence of the in vitro E3 ubiquitin ligase activity and cisplatin sensitivity of the missense mutation D67Y BRCA1 RING domain. The D67Y BRCA1 RING domain protein exhibited the reduced ubiquitination function, and was more susceptible to the drug than the D67E or wild-type BRCA1 RING domain protein. This evidence emphasized the potential of using the BRCA1 dysfunction as an important determinant of chemotherapy responses in breast cancer.

scholarly journals Mind Bomb-2 Is an E3 Ligase for Notch Ligand

2005 ◽  
Vol 280 (23) ◽  
pp. 22335-22342 ◽  
Author(s):  
Bon-Kyoung Koo ◽  
Ki-Jun Yoon ◽  
Kyeong-Won Yoo ◽  
Hyoung-Soo Lim ◽  
Ran Song ◽  
...  
Keyword(s):  
Notch Signaling ◽  
Ubiquitin Ligase ◽  
Mouse Genome ◽  
E3 Ubiquitin Ligase ◽  
Membrane Localization ◽  
Notch Ligand ◽  
Adult Tissues ◽  
Ubiquitin Ligase Activity ◽  
Evolutionarily Conserved ◽  
Intracellular Vesicles

The zebrafish gene, mind bomb (mib), encodes a protein that positively regulates of the Delta-mediated Notch signaling. It interacts with the intracellular domain of Delta to promote its ubiquitination and endocytosis. In our search for the mouse homologue of zebrafish mind bomb, we cloned two homologues in the mouse genome: a mouse orthologue (mouse mib1) and a paralogue, named mind bomb-2 (mib2), which is evolutionarily conserved from Drosophila to human. Both Mib1 and Mib2 have an E3 ubiquitin ligase activity in their C-terminal RING domain and interact with Xenopus Delta (XD) via their N-terminal region. Mib2 is also able to ligate ubiquitin to XD and shift the membrane localization of Delta to intracellular vesicles. Importantly, Mib2 rescues both the neuronal and vascular defects in the zebrafish mibta52b mutants. In contrast to the functional similarities between Mib1 and Mib2, mib2 is highly expressed in adult tissues, but almost not at all in embryos, whereas mib1 is abundantly expressed in both embryos and adult tissues. These data suggest that Mib2 has functional similarities to Mib1, but might have distinct roles in Notch signaling as an E3 ubiquitin ligase.

scholarly journals The E3 Ubiquitin Ligase Mindbomb1 controls zebrafish Planar Cell Polarity

2021 ◽  
Author(s):  
Vishnu Muraleedharan Saraswathy ◽  
Priyanka Sharma ◽  
Akshai Janardhana Kurup ◽  
Sophie Polès ◽  
Morgane Poulain ◽  
...  
Keyword(s):  
Notch Signaling ◽  
Cell Polarity ◽  
Ubiquitin Ligase ◽  
Protein Trafficking ◽  
Planar Cell Polarity ◽  
E3 Ubiquitin Ligase ◽  
Notch Pathway ◽  
Ring Finger ◽  
Critical Event ◽  
Loss Of Function

Vertebrate Delta/Notch signaling involves multiple ligands, receptors and transcription factors. Delta endocytosis – a critical event for Notch activation – is however essentially controlled by the E3 Ubiquitin ligase Mindbomb1 (Mib1). Due to its position at a molecular bottleneck of the pathway, Mib1 inactivation is often used to inhibit Notch signaling. However, recent findings indicate that the importance of Mib1 extends beyond the Notch pathway. We report an essential role of Mib1 in Planar Cell Polarity (PCP). mib1 null mutants or morphants display impaired gastrulation stage Convergence Extension (CE) movements. Comparison of different mib1 mutants and functional rescue experiments indicate that Mib1 controls CE independently of Notch. In contrast, Mib1-dependent CE defects can be rescued using the PCP downstream mediator RhoA. Mib1 regulates CE through the RING Finger domains that have been implicated in substrate ubiquitination, suggesting that Mib1 may control PCP protein trafficking. Accordingly, we show that Mib1 controls the endocytosis of the PCP component Ryk and that Ryk internalization is required for CE. Numerous morphogenetic processes involve both Notch and PCP signaling. We show that Mib1, a known Notch signaling regulator, is also an essential PCP pathway component. Care should therefore be taken when interpreting Mib1 loss of function phenotypes.

scholarly journals UBR-5, a Conserved HECT-Type E3 Ubiquitin Ligase, Negatively Regulates Notch-Type Signaling in Caenorhabditis elegans

2016 ◽  
Vol 6 (7) ◽  
pp. 2125-2134 ◽  
Author(s):  
Komal Safdar ◽  
Anniya Gu ◽  
Xia Xu ◽  
Vinci Au ◽  
Jon Taylor ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase

scholarly journals SPIN1, a K Homology Domain Protein Negatively Regulated and Ubiquitinated by the E3 Ubiquitin Ligase SPL11, Is Involved in Flowering Time Control in Rice

2008 ◽  
Vol 20 (6) ◽  
pp. 1456-1469 ◽  
Author(s):  
Miguel E. Vega-Sánchez ◽  
Lirong Zeng ◽  
Songbiao Chen ◽  
Hei Leung ◽  
Guo-Liang Wang
Keyword(s):  
Flowering Time ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Time Control ◽  
Domain Protein ◽  
Flowering Time Control

scholarly journals Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

2001 ◽  
Vol 11 (20) ◽  
pp. 1569-1577 ◽  
Author(s):  
Jens Demand ◽  
Simon Alberti ◽  
Cam Patterson ◽  
Jörg Höhfeld
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Domain Protein
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