ATR:ATRIP:RPA:ssDNA signaling complex [nucleoplasm]

Stable Identifier
Homo sapiens
ATR-ATRIP-RPA-ssDNA signaling complex
Locations in the PathwayBrowser
While the ATR-ATRIP complex binds only poorly to RPA complexed with ssDNA lengths of 30 or 50 nt, binding is significantly enhanced in the presence of a 75 nt ssDNA molecule. Complex formation is primarily mediated by physical interaction between ATRIP and RPA. Multiple elements within the ATRIP molecule can bind to the RPA-ssDNA complex, including residues 1-107 (highest affinity), 218-390, and 390-791 (lowest afiinity). Although the full-length ATRIP is unable to bind ssDNA, an internal region (108-390) can weakly bind ssDNA when present in rabbit reticulocyte lysates. ATR can bind to the ssDNA directly independent of RPA, but this binding is inhibited by ATRIP. Upon binding, the ATR kinase becomes activated and can directly phosphorylate substrates such as Rad17.
Literature References
PubMed ID Title Journal Year
16314342 DNA damage checkpoints in mammals

Niida, H, Nakanishi, M

Mutagenesis 2005
12791985 Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes

Zou, L, Elledge, SJ

Science 2003
16407120 ATRIP associates with replication protein A-coated ssDNA through multiple interactions

Zou, L, Namiki, Y

Proc Natl Acad Sci U S A 2006
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