The BRCA1/BARD1 Heterodimer Assembles Polyubiquitin Chains through an Unconventional Linkage Involving Lysine Residue K6 of Ubiquitin*
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Summary
The ability of BRCA1/BARD1 to form K6-linked polyubiquitin chains suggests that it may impart unique cellular properties to its natural enzymatic substrates.
- Type
- article
- Published
- 2003-09-12
- Cited by
- 320
- References
- 29
- Access
- Open access
- OpenAlex
- https://openalex.org/W2045128403
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:38095850
Keywords
Ubiquitin, Ubiquitin ligase, Lysine, Chemistry, Biochemistry
References
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- Structure of a BRCA1–BARD1 heterodimeric RING–RING complex
- Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex
- Functional communication between endogenous BRCA1 and its partner, BARD1, during Xenopus laevis development
- RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination.
- Cancer-predisposing mutations within the RING domain of BRCA1: Loss of ubiquitin protein ligase activity and protection from radiation hypersensitivity
- Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
- Identification of a RING protein that can interact in vivo with the BRCA1 gene product
- Novel Multiubiquitin Chain Linkages Catalyzed by the Conjugating Enzymes E2EPF and RAD6 Are Recognized by 26 S Proteasome Subunit 5 (*)
- Enhancement of BRCA1 E3 Ubiquitin Ligase Activity through Direct Interaction with the BARD1 Protein*
- The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity.
- A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein.
- The RING Heterodimer BRCA1-BARD1 Is a Ubiquitin Ligase Inactivated by a Breast Cancer-derived Mutation*
Cited by
- The ubiquitin-proteasome pathway and its role in cancer.
- Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair.
- The ubiquitin proteasome system in neurodegenerative diseases: culprit, accomplice or victim?
- The RING Finger Protein RNF8 Ubiquitinates Nbs1 to Promote DNA Double-strand Break Repair by Homologous Recombination*
- Analyse de l'expression de BARD1 dans le cancer du poumon et le cancer colorectal
- Studies on RNF8, a ubiquitin ligase with a RING finger domain
- Defining the regulation and function of SAFB1 and SAFB2 in human breast cancer cells
- Manipulation of the ubiquitin-proteasome system by HIV-1 : role of the accessory protein Vpr
- Signalling functions of polyubiquitin chains and ubiquitin-binding domains
- Etude de l'effet antitumoral de l'activation de la NO-synthase inductible dans un modèle de cancer du sein : analyse des mécanismes moléculaires
- The Role of BRCA1 in DNA Double-strand Break Repair
- Characterisation of deubiquitinase enzymes involved in androgen receptor regulation in prostate cancer
- ATM, BRCA1, and Aurora A: Mechanisms of G2/M Checkpoint Control in Human Embryonic Stem Cells
- Characterization of the Ubc13-Mms2 Lysine-63-linked ubiquitin conjugating complex
- Implications of BRCA1 mutations in basal-like breast cancer development and treatment
- Chemical and genetic strategies for manipulating polyubiquitin chain structure.
- Controlled synthesis of polyubiquitin chains.
- DNA repair by HDR in experimental tumorigenesis
- Accumulation of polyubiquitinated proteins by overexpression of RBCC protein interacting with protein kinase C2, a splice variant of ubiquitin ligase RBCC protein interacting with protein kinase C1
- Regulation of Estrogen Receptor alpha Ubiquitination and Proteasome-mediated Receptor Degradation
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