Sandra Zinkel
Assistant Professor of Medicine
Last active: 3/26/2019

BID binds to replication protein A and stimulates ATR function following replicative stress.

Liu Y, Vaithiyalingam S, Shi Q, Chazin WJ, Zinkel SS
Mol Cell Biol. 2011 31 (21): 4298-309

PMID: 21859891 · PMCID: PMC3209332 · DOI:10.1128/MCB.05737-11

Proapoptotic BH3-interacting death domain agonist (BID) regulates apoptosis and the DNA damage response. Following replicative stress, BID associates with proteins of the DNA damage sensor complex, including replication protein A (RPA), ataxia telangiectasia and Rad3 related (ATR), and ATR-interacting protein (ATRIP), and facilitates an efficient DNA damage response. We have found that BID stimulates the association of RPA with components of the DNA damage sensor complex through interaction with the basic cleft of the N-terminal domain of the RPA70 subunit. Disruption of the BID-RPA interaction impairs the association of ATR-ATRIP with chromatin as well as ATR function, as measured by CHK1 activation and recovery of DNA replication following hydroxyurea (HU). We further demonstrate that the association of BID with RPA stimulates the association of ATR-ATRIP to the DNA damage sensor complex. We propose a model in which BID associates with RPA and stimulates the recruitment and/or stabilization of ATR-ATRIP to the DNA damage sensor complex.

MeSH Terms (27)

Adaptor Proteins, Signal Transducing Amino Acid Sequence Apoptosis Ataxia Telangiectasia Mutated Proteins Base Sequence BH3 Interacting Domain Death Agonist Protein Cell Cycle Proteins Cell Line DNA-Binding Proteins DNA Damage DNA Replication Humans Models, Biological Models, Molecular Molecular Sequence Data Multiprotein Complexes Mutagenesis, Site-Directed Nuclear Magnetic Resonance, Biomolecular Proliferating Cell Nuclear Antigen Protein-Serine-Threonine Kinases Protein Binding Protein Interaction Domains and Motifs Recombinant Proteins Replication Protein A RNA, Small Interfering Signal Transduction Stress, Physiological

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