Search results for RPA2

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Reaction (8 results from a total of 8)

Identifier: R-HSA-5687758
Species: Homo sapiens
Compartment: nucleoplasm
The protein serine/threonine phosphatase complex composed of a catalytic subunit PPP4C (PP4C) and a regulatory subunit PPP4R2 (PP4R2) dephosphorylates serine S33 of the RPA2 subunit of the RPA heterotrimer. By regulating the availability of unphosphorylated RPA2, PPP4C:PPP4R2 phosphatase regulates the progression of the homologous recombination repair of DNA double strand breaks and the duration of ATR checkpoint signaling (Lee et al. 2010).
Identifier: R-HSA-5685156
Species: Homo sapiens
Compartment: nucleoplasm
Activated ATR phosphorylates the RPA2 subunit of the RPA complex on serine residue S33. Phosphorylation of RPA2 at S33 likely stimulates additional RPA2 phosphorylation on CDK sites (S23 and S29) and DNA-PKcs (PRKDC) sites (S4, S8 and S21). DNA damage-regulated phosphorylation of RPA2 plays an important role in the progression of homologous recombination-directed repair of DNA double strand breaks (DSBs) (Anantha et al. 2007, Liu et al. 2012, Murphy et al. 2014)
Identifier: R-HSA-6788392
Species: Homo sapiens
Compartment: nucleoplasm
ATR phosphorylates several proteins at DNA insterstrand crosslinks (ICL-DNA), with ATR activity at ICL-DNA being independent of the presence of RAD17 and TOPBP1 (Shigechi et al. 2012, Tomida et al. 2013). Besides phosphorylating the RPA2 subunit of the RPA heterotrimeric complex (Huang et al. 2010), activated ATR also phosphorylates the Fanconi anemia core complex component FANCM on serine residue S1045 (Singh et al. 2013). ATR-mediated phosphorylation of FANCM is thought to be important for the progression of ICL repair, although the mechanism is not known. The critical ATR substrate at ICL-DNA is considered to be FANCI component of the ID2 complex. ATR-mediated phosphorylation of FANCI, at least on serine residues S556, S559, S565 and S617, is a prerequisite for FANCD2 monoubiquitination (Ishiai et al. 2008, Shigechi et al. 2012). FANDC2 itself is also phosphorylated by ATR on threonine residue T691 and serine residue S717, which promotes FANCD2 monoubiquitination and enhances cellular resistance to DNA crosslinking agents (Ho et al. 2006).
Identifier: R-HSA-5684875
Species: Homo sapiens
Compartment: nucleoplasm
ATR (ATM- and rad3-related) kinase is an essential checkpoint factor in human cells constitutively associated with ATRIP (ATR-interacting protein). The ATR:ATRIP complex binds RPA complex (RPA1:RPA2:RPA3) associated with ssDNA at resected DNA double strand breaks (DSBs). Complex formation is primarily mediated by physical interaction between ATRIP and RPA1 (Zou and Elledge 2003, Jazayeri et al. 2006).
Identifier: R-HSA-5684882
Species: Homo sapiens
Compartment: nucleoplasm
The recruitment of CHEK1 (CHK1) to resected DNA double strand breaks (DSBs) and activation by ATR-mediated phosphorylation requires the presence of CLSPN (claspin) and TIMELESS:TIPIN protein complex. TIPIN simultaneously interacts with the RPA2 subunit of the RPA complex and CLSPN, allowing CLSPN to stably associate with resected DNA DSBs (Kemp et al. 2010). Phosphorylation of CLSPN at threonine T916 and serine S945 is needed for CHEK1 binding (Kumagai et al. 2003, Clarke and Clarke 2005). CLSPN phosphorylation at these sites is independent of CHEK1 (Bennett et al. 2008). Casein kinase 1 (CK1) was proposed as a kinase responsible for CLSPN phosphorylation (Meng et al. 2011) but the exact mechanism of this modification has not been established.

ATR-mediated phosphorylation of RAD17 on serine residues S635 and S645 is implicated in CLSPN recruitment to resected DNA DSBs and CLSPN phosphorylation (Wang et al. 2006). Also, phosphorylation of the RPA2 subunit of the RPA complex positively contributes to CHEK1 activation (Liu et al. 2012).

Identifier: R-HSA-9007447
Species: Homo sapiens
Compartment: nucleoplasm
E2F6 forms a complex with CBX3 (HP1gamma) and components of the polycomb repressor complex PRC1.6: PCGF6 (MBLR), L3MBTL2, RING1 (RING1A) or RNF2 (RING2, also known as RING2B). This polycomb repressor-like complex is named PRC1L4. Unlike the complex composed of E2F6.com-1, PRC1.6 and CBX3 (Ogawa et al. 2002), the PRC1L4 complex does not possess histone methyltransferase activity. Instead, the PRC1L4 complex may have a histone E3-ubiquitin ligase activity. The PRC1L4 complex was shown to bind to promoters of several genes: CDC7, CSTF3, MCM3, UXT, RPA2, RAD51C, RFC3, HOXC5. Of these genes, transcriptional repression was tested and demonstrated for CDC7 and UXT (Trojer et al. 2011).
Identifier: R-HSA-5689317
Species: Homo sapiens
Compartment: nucleoplasm
Once an open bubble structure is generated in damaged dsDNA through a DNA helicase activity of the TFIIH complex, the RPA heterotrimer composed of RPA1, RPA2 and RPA3, coats the undamaged single strand DNA (ssDNA) (de Laat et al. 1998), thereby protecting it from incision and enabling the correct positioning of the NER endonucleases. The interaction of RPA with XPA facilitates RPA recruitment to the global genome nucleotide excision repair (GG-NER) site (He et al. 1995, Ikegami et al. 1998). A DNA endonuclease ERCC5 (XPG) is recruited to the GG-NER site, 3' to the DNA damage, through its interaction with the TFIIH complex (Dunand-Sauthier et al. 2005, Zotter et al. 2006, Ito et al. 2007) and the RPA heterotrimer (de Laat et al. 1998).
Identifier: R-HSA-6782138
Species: Homo sapiens
Compartment: nucleoplasm
It has been suggested that, similar to the UvrD helicase involved in TC-NER in E.coli, the DNA helicase activity of TFIIH complex may facilitate damage-stalled RNA polymerase II (RNA Pol II) backtracking (Epshtein et al. 2014). RNA Pol II backtracking, together with the cleavage of the 3' protruding end of nascent mRNA, might promote the movement of the transcription bubble away from the transcription-coupled nucleotide excision repair (TC-NER) site, while an open bubble is created (Sarker et al. 2005, Hanawalt and Spivak 2008). Once the open bubble is generated, the RPA heterotrimer composed of RPA1, RPA2 and RPA3 coats the undamaged single strand DNA (ssDNA) (de Laat et al. 1998), thereby protecting it from endonucleases. The interaction of RPA with XPA facilitates RPA recruitment to the nucleotide excision repair (NER) site (He et al. 1995, Ikegami et al. 1998). A DNA endonuclease ERCC5 (XPG) is recruited to the TC-NER site through its interaction with the stalled RNA Pol II (Sarker et al. 2005), the TFIIH complex (Dunand-Sauthier et al. 2005, Zotter et al. 2006, Ito et al. 2007) and the RPA heterotrimer (de Laat et al. 1998).
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