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n2:pmcid: PMC0
bibo:doi: 10.1083%2Fjcb.201005101
n9:contains: _:vb8944687 _:vb8944650 _:vb8944669

Subject Item: _:vb8944650
rdf:type: n9:Section
dc:title: introduction
n9:contains: _:vb8944652 _:vb8944653 _:vb8944654 _:vb8944655 _:vb8944651 _:vb8944668 _:vb8944664 _:vb8944665 _:vb8944666 _:vb8944667 _:vb8944660 _:vb8944661 _:vb8944662 _:vb8944663 _:vb8944656 _:vb8944657 _:vb8944658 _:vb8944659

Subject Item: _:vb8944651
rdf:type: n2:Context
rdf:value: To date, 13 FA genetic complementation groups have been identified (Moldovan and D’Andrea, >>2009<<). Consistent with the sensitivity to ICLs, the proteins encoded by the FANC genes repair these lesions. Although the molecular and biochemical functions of the FA pathway remain poorly understood, the following model has emerged. In
n2:mentions: n3:19686080

Subject Item: _:vb8944652
rdf:type: n2:Context
rdf:value: In response to ICLs and replication stress, FANCM and FAAP24 are recruited to replication forks stalled either by ICLs or other forms of replication stress (Ciccia et al., >>2007<<; Kim et al., 2008).
n2:mentions: n3:17289582

Subject Item: _:vb8944653
rdf:type: n2:Context
rdf:value: In response to ICLs and replication stress, FANCM and FAAP24 are recruited to replication forks stalled either by ICLs or other forms of replication stress (Ciccia et al., 2007; Kim et al., >>2008<<). The FANCM–FAAP24 complex promotes chromatin loading of the FA core complex (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, and FAAP100), which contains FA complementation group L (FANCL) protein, an E3 ubiquitin ligase. FANCL and
n2:mentions: n3:18174376

Subject Item: _:vb8944654
rdf:type: n2:Context
rdf:value: Ubiquitylation of the ID complex targets it to the stalled replication fork or site of damage, where it promotes processing and repair of the ICL lesion (Räschle et al., >>2008<<; Knipscheer et al., 2009; Kratz et al., 2010; Smogorzewska et al., 2010).
n2:mentions: n3:18805090

Subject Item: _:vb8944655
rdf:type: n2:Context
rdf:value: Ubiquitylation of the ID complex targets it to the stalled replication fork or site of damage, where it promotes processing and repair of the ICL lesion (Räschle et al., 2008; Knipscheer et al., >>2009<<; Kratz et al., 2010; Smogorzewska et al., 2010).
n2:mentions: n3:19965384

Subject Item: _:vb8944656
rdf:type: n2:Context
rdf:value: Ubiquitylation of the ID complex targets it to the stalled replication fork or site of damage, where it promotes processing and repair of the ICL lesion (Räschle et al., 2008; Knipscheer et al., 2009; Kratz et al., >>2010<<; Smogorzewska et al., 2010).
n2:mentions: n3:20603016

Subject Item: _:vb8944657
rdf:type: n2:Context
rdf:value: of the ID complex targets it to the stalled replication fork or site of damage, where it promotes processing and repair of the ICL lesion (Räschle et al., 2008; Knipscheer et al., 2009; Kratz et al., 2010; Smogorzewska et al., >>2010<<).
n2:mentions: n3:20603073

Subject Item: _:vb8944658
rdf:type: n2:Context
rdf:value: ICLs and other forms of replication stress also activate the translesion synthesis (TLS) pathway (Lee and Myung, >>2008<<), which is initiated by the recruitment of the RAD18–RAD6 complex, an E3 ubiquitin ligase and an E2 ubiquitin–conjugating enzyme pair.
n2:mentions: n3:18525240

Subject Item: _:vb8944659
rdf:type: n2:Context
rdf:value: a known role in the recruitment and regulation of TLS polymerases, which, because of large active sites, have reduced fidelity but increased ability to synthesize over lesions that stall the high fidelity DNA polymerases (Guo et al., >>2009<<). Genetic data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., 2006; Shen et al.
n2:mentions: n3:19367366

Subject Item: _:vb8944660
rdf:type: n2:Context
rdf:value: Genetic data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., >>2002<<; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., 2006; Shen et al., 2006; Simpson et al., 2006; Saberi et al., 2007).
n2:mentions: n3:12374756

Subject Item: _:vb8944661
rdf:type: n2:Context
rdf:value: Genetic data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., >>2003<<; Nojima et al., 2005; Arakawa et al., 2006; Shen et al., 2006; Simpson et al., 2006; Saberi et al., 2007).
n2:mentions: n3:12509447

Subject Item: _:vb8944662
rdf:type: n2:Context
rdf:value: Genetic data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., >>2005<<; Arakawa et al., 2006; Shen et al., 2006; Simpson et al., 2006; Saberi et al., 2007).
n2:mentions: n3:16357182

Subject Item: _:vb8944663
rdf:type: n2:Context
rdf:value: Genetic data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., >>2006<<; Shen et al., 2006; Simpson et al., 2006; Saberi et al., 2007).
n2:mentions: n3:17105346

Subject Item: _:vb8944664
rdf:type: n2:Context
rdf:value: data demonstrate that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., 2006; Shen et al., >>2006<<; Simpson et al., 2006; Saberi et al., 2007). However, these roles remain poorly understood.
n2:mentions: n3:16571727

Subject Item: _:vb8944665
rdf:type: n2:Context
rdf:value: that RAD18 and PCNA ubiquitylation also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., 2006; Shen et al., 2006; Simpson et al., >>2006<<; Saberi et al., 2007). However, these roles remain poorly understood.
n2:mentions: n3:16888649

Subject Item: _:vb8944666
rdf:type: n2:Context
rdf:value: also play critical roles in cells challenged with agents that induce ICLs (Yamashita et al., 2002; Tateishi et al., 2003; Nojima et al., 2005; Arakawa et al., 2006; Shen et al., 2006; Simpson et al., 2006; Saberi et al., >>2007<<). However, these roles remain poorly understood.
n2:mentions: n3:17242200

Subject Item: _:vb8944667
rdf:type: n2:Context
rdf:value: One function for ubiquitylated PCNA in the repair of ICLs is to recruit or regulate the TLS DNA polymerases REV1 and polymerase ζ, which are required for ICL repair (Sarkar et al., >>2006<<; Shen et al., 2006).
n2:mentions: n3:16482220

Subject Item: _:vb8944668
rdf:type: n2:Context
rdf:value: One function for ubiquitylated PCNA in the repair of ICLs is to recruit or regulate the TLS DNA polymerases REV1 and polymerase ζ, which are required for ICL repair (Sarkar et al., 2006; Shen et al., >>2006<<). Nevertheless, PCNA ubiquitylation may have a previously unknown function in the regulation of the FA pathway. Consistent with this later possibility, we report in this study that RAD18-mediated PCNA ubiquitylation plays a pivotal role
n2:mentions: n3:16571727

Subject Item: _:vb8944669
rdf:type: n9:Section
dc:title: materials and methods
n9:contains: _:vb8944670 _:vb8944671 _:vb8944672 _:vb8944673 _:vb8944674 _:vb8944675 _:vb8944676 _:vb8944677 _:vb8944678 _:vb8944679 _:vb8944680 _:vb8944681 _:vb8944682 _:vb8944683 _:vb8944684 _:vb8944685 _:vb8944686

Subject Item: _:vb8944670
rdf:type: n2:Context
rdf:value: HeLa and K562 cells obtained from American Type Culture Collection were grown and transfected by electroporation as described previously (Arlander et al., >>2003<<) and were used 48 or 72 h after transfection as indicated. Cell cycle analyses (Arlander et al., 2003) and clonogenic assays (Wagner and Karnitz, 2009) were performed as described previously.
n2:mentions: n3:14570880

Subject Item: _:vb8944671
rdf:type: n2:Context
rdf:value: Cell cycle analyses (Arlander et al., >>2003<<) and clonogenic assays (Wagner and Karnitz, 2009) were performed as described previously.
n2:mentions: n3:14570880

Subject Item: _:vb8944672
rdf:type: n2:Context
rdf:value: Cell cycle analyses (Arlander et al., 2003) and clonogenic assays (Wagner and Karnitz, >>2009<<) were performed as described previously.
n2:mentions: n3:19403702

Subject Item: _:vb8944673
rdf:type: n2:Context
rdf:value: Shiomi (National Institute of Radiological Sciences, Chiba, Japan) and grown as described previously (Shiomi et al., >>2007<<).
n2:mentions: n3:17158148

Subject Item: _:vb8944674
rdf:type: n2:Context
rdf:value: Wang, National Institutes of Health, Bethesda, MD), ORC2 (BD), β-actin (Sigma-Aldrich), HA tag (Covance), S tag (Hackbarth et al., >>2004<<), and Flag tag (Flag M1 mAb; Sigma-Aldrich).
n2:mentions: n3:15560139

Subject Item: _:vb8944675
rdf:type: n2:Context
rdf:value: 5′-GCUCUCUGAUCGUGAUUUA-3′; RAD18-3, 5′-GCAGUUUGCUUUAGAGUCA-3′; RAD18-4, 5′-AUAACCGCAUAUUAGAUGA-3′; RAD18-5, 5′-CCAAGAAACAAGCGUAAUA-3′; RAD18-6, 5′-GGAGCAGGUUAAUGGAUAA-3′; luciferase, 5′-CUUACGCUGAGUACUUCGA-3′ (Elbashir et al., >>2001<<); FANCD2, 5′-GGUCAGAGCUGUAUUAUUC-3′ (Wagner and Karnitz, 2009); PCNA, 5′-GGAGAAAGUUUCAGACUAU-3′ (Merkerova et al., 2007); and FANCL, 5′-GACAAGAGCUGUAUGCACU-3′ (Meetei et al., 2003).
n2:mentions: n3:11373684

Subject Item: _:vb8944676
rdf:type: n2:Context
rdf:value: RAD18-4, 5′-AUAACCGCAUAUUAGAUGA-3′; RAD18-5, 5′-CCAAGAAACAAGCGUAAUA-3′; RAD18-6, 5′-GGAGCAGGUUAAUGGAUAA-3′; luciferase, 5′-CUUACGCUGAGUACUUCGA-3′ (Elbashir et al., 2001); FANCD2, 5′-GGUCAGAGCUGUAUUAUUC-3′ (Wagner and Karnitz, >>2009<<); PCNA, 5′-GGAGAAAGUUUCAGACUAU-3′ (Merkerova et al., 2007); and FANCL, 5′-GACAAGAGCUGUAUGCACU-3′ (Meetei et al., 2003).
n2:mentions: n3:19403702

Subject Item: _:vb8944677
rdf:type: n2:Context
rdf:value: RAD18-6, 5′-GGAGCAGGUUAAUGGAUAA-3′; luciferase, 5′-CUUACGCUGAGUACUUCGA-3′ (Elbashir et al., 2001); FANCD2, 5′-GGUCAGAGCUGUAUUAUUC-3′ (Wagner and Karnitz, 2009); PCNA, 5′-GGAGAAAGUUUCAGACUAU-3′ (Merkerova et al., >>2007<<); and FANCL, 5′-GACAAGAGCUGUAUGCACU-3′ (Meetei et al., 2003).
n2:mentions: n3:17070905

Subject Item: _:vb8944678
rdf:type: n2:Context
rdf:value: 5′-CUUACGCUGAGUACUUCGA-3′ (Elbashir et al., 2001); FANCD2, 5′-GGUCAGAGCUGUAUUAUUC-3′ (Wagner and Karnitz, 2009); PCNA, 5′-GGAGAAAGUUUCAGACUAU-3′ (Merkerova et al., 2007); and FANCL, 5′-GACAAGAGCUGUAUGCACU-3′ (Meetei et al., >>2003<<).
n2:mentions: n3:12973351

Subject Item: _:vb8944679
rdf:type: n2:Context
rdf:value: The FANCL expression plasmids were created by ligating PCR-amplified FANCL into vectors that append an N-terminal SFB tag (pSFB; Chini and Chen, >>2006<<), an N-terminal S tag (pSPN; Hackbarth et al., 2004), or a C-terminal tandem HA tag (pcDNA3-HA2; Volkmer and Karnitz, 1999).
n2:mentions: n3:16963448

Subject Item: _:vb8944680
rdf:type: n2:Context
rdf:value: The FANCL expression plasmids were created by ligating PCR-amplified FANCL into vectors that append an N-terminal SFB tag (pSFB; Chini and Chen, 2006), an N-terminal S tag (pSPN; Hackbarth et al., >>2004<<), or a C-terminal tandem HA tag (pcDNA3-HA2; Volkmer and Karnitz, 1999). The S-PCNA expression vector was constructed by ligating PCR-amplified PCNA into pSPC, which appends a C-terminal S tag (Hackbarth et al., 2004).
n2:mentions: n3:15560139

Subject Item: _:vb8944681
rdf:type: n2:Context
rdf:value: created by ligating PCR-amplified FANCL into vectors that append an N-terminal SFB tag (pSFB; Chini and Chen, 2006), an N-terminal S tag (pSPN; Hackbarth et al., 2004), or a C-terminal tandem HA tag (pcDNA3-HA2; Volkmer and Karnitz, >>1999<<). The S-PCNA expression vector was constructed by ligating PCR-amplified PCNA into pSPC, which appends a C-terminal S tag (Hackbarth et al., 2004).
n2:mentions: n3:9872989

Subject Item: _:vb8944682
rdf:type: n2:Context
rdf:value: The S-PCNA expression vector was constructed by ligating PCR-amplified PCNA into pSPC, which appends a C-terminal S tag (Hackbarth et al., >>2004<<). S-PCNA K164R was derived from pSPC-PCNA by site-directed mutagenesis. PCNA expression plasmids resistant to the siRNA, four silent mutations (identified by underlines), were generated using the oligonucleotide
n2:mentions: n3:15560139

Subject Item: _:vb8944683
rdf:type: n2:Context
rdf:value: The plasmid pET25b-hRAD18-His6hHR6B, which was used to express the RAD18–RAD6B complex in E. coli, has been described previously (Notenboom et al., >>2007<<) and was provided by T.
n2:mentions: n3:17720710

Subject Item: _:vb8944684
rdf:type: n2:Context
rdf:value: The biochemical fractionation of soluble and chromatin-bound proteins was performed as described previously (Geng et al., >>2007<<). For immunoprecipitations, cells were lysed in 20 mM Tris, pH 7.4, 150 mM NaCl, 5 mM MgCl2, 1% Triton X-100 supplemented with 5 mM CaCl2, 300 U/ml micrococcal nuclease, 10 mM N-ethylmaleimide, 10 µg/ml leupeptin, 5 µg/ml pepstatin, 20 nM
n2:mentions: n3:17242184

Subject Item: _:vb8944685
rdf:type: n2:Context
rdf:value: GST pull-down experiments were performed as described previously (Bienko et al., >>2005<<) using proteins obtained as follows: GST, GST-PCNA, His6-PCNA, and GST-FANCL (amino acids 1–306) were purified from E. coli using glutathione agarose (Thermo Fisher Scientific) or TALON Superflow metal affinity resin (Takara Bio Inc.
n2:mentions: n3:16357261

Subject Item: _:vb8944686
rdf:type: n2:Context
rdf:value: To prepare in vitro–ubiquitylated PCNA, 100 ng purified GST-PCNA or GST-PCNAK164R was incubated with 50 ng rabbit E1 ubiquitin–activating enzyme (EMD) and 350 ng hRAD18-RAD6 (prepared as described previously in Notenboom et al. [>>2007<<]) with or without 5 µg HA-tagged human ubiquitin (Boston Biochem) in ubiquitination reaction buffer (50 mM Tris, pH 7.4, 5 mM MgCl2, 2 mM ATP, 2 µM ZnCl2, 2 mM NaF, and 0.6 mM DTT) at 30°C for 1 h.
n2:mentions: n3:17720710

Subject Item: _:vb8944687
rdf:type: n9:Section
dc:title: results and discussion
n9:contains: _:vb8944704 _:vb8944705 _:vb8944706 _:vb8944707 _:vb8944708 _:vb8944696 _:vb8944697 _:vb8944698 _:vb8944699 _:vb8944700 _:vb8944701 _:vb8944702 _:vb8944703 _:vb8944688 _:vb8944689 _:vb8944690 _:vb8944691 _:vb8944692 _:vb8944693 _:vb8944694 _:vb8944695

Subject Item: _:vb8944688
rdf:type: n2:Context
rdf:value: Previous studies demonstrated that both RAD18 and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., >>2002<<; Nojima et al., 2005; Ross et al., 2005; Lee and Myung, 2008; Wagner and Karnitz, 2009; Hicks et al., 2010).
n2:mentions: n3:12374756

Subject Item: _:vb8944689
rdf:type: n2:Context
rdf:value: Previous studies demonstrated that both RAD18 and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., 2002; Nojima et al., >>2005<<; Ross et al., 2005; Lee and Myung, 2008; Wagner and Karnitz, 2009; Hicks et al., 2010).
n2:mentions: n3:16357182

Subject Item: _:vb8944690
rdf:type: n2:Context
rdf:value: Previous studies demonstrated that both RAD18 and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., 2002; Nojima et al., 2005; Ross et al., >>2005<<; Lee and Myung, 2008; Wagner and Karnitz, 2009; Hicks et al., 2010).
n2:mentions: n3:15741181

Subject Item: _:vb8944691
rdf:type: n2:Context
rdf:value: Previous studies demonstrated that both RAD18 and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., 2002; Nojima et al., 2005; Ross et al., 2005; Lee and Myung, >>2008<<; Wagner and Karnitz, 2009; Hicks et al., 2010).
n2:mentions: n3:18525240

Subject Item: _:vb8944692
rdf:type: n2:Context
rdf:value: that both RAD18 and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., 2002; Nojima et al., 2005; Ross et al., 2005; Lee and Myung, 2008; Wagner and Karnitz, >>2009<<; Hicks et al., 2010).
n2:mentions: n3:19403702

Subject Item: _:vb8944693
rdf:type: n2:Context
rdf:value: and FANCD2 play important roles in eukaryotic cells exposed to cisplatin and other DNA cross-linking agents (Yamashita et al., 2002; Nojima et al., 2005; Ross et al., 2005; Lee and Myung, 2008; Wagner and Karnitz, 2009; Hicks et al., >>2010<<). In our experiments to understand the DNA repair pathways that affect the sensitivity of human tumor cells to cisplatin, a chemotherapy agent that causes ICL formation (Wang and Lippard, 2005), we depleted HeLa cells of FANCD2, a key
n2:mentions: n3:20028736

Subject Item: _:vb8944694
rdf:type: n2:Context
rdf:value: In our experiments to understand the DNA repair pathways that affect the sensitivity of human tumor cells to cisplatin, a chemotherapy agent that causes ICL formation (Wang and Lippard, >>2005<<), we depleted HeLa cells of FANCD2, a key participant in the FA repair pathway, and of RAD18, a regulator of the TLS pathway (Fig.
n2:mentions: n3:15789122

Subject Item: _:vb8944695
rdf:type: n2:Context
rdf:value: S1 B), which creates bulky DNA lesions that are bypassed by TLS polymerases after RAD18-mediated PCNA ubiquitylation (Tateishi et al., >>2000<<; Kannouche et al., 2004; Watanabe et al., 2004).
n2:mentions: n3:10884424

Subject Item: _:vb8944696
rdf:type: n2:Context
rdf:value: S1 B), which creates bulky DNA lesions that are bypassed by TLS polymerases after RAD18-mediated PCNA ubiquitylation (Tateishi et al., 2000; Kannouche et al., >>2004<<; Watanabe et al., 2004).
n2:mentions: n3:15149598

Subject Item: _:vb8944697
rdf:type: n2:Context
rdf:value: S1 B), which creates bulky DNA lesions that are bypassed by TLS polymerases after RAD18-mediated PCNA ubiquitylation (Tateishi et al., 2000; Kannouche et al., 2004; Watanabe et al., >>2004<<). Surprisingly, however, codepletion of both proteins did not cause a more profound sensitization to cisplatin. Given that the RAD18 and FANCD2 depletions were both highly effective, this result raised the possibility that these proteins
n2:mentions: n3:15359278

Subject Item: _:vb8944698
rdf:type: n2:Context
rdf:value: S1 D) and reduced the cisplatin-induced binding of FANCD2 to chromatin, an event that depends on FANCD2 ubiquitylation (Wang et al., >>2004<<), in K562 (Fig.
n2:mentions: n3:15199141

Subject Item: _:vb8944699
rdf:type: n2:Context
rdf:value: We therefore asked whether PCNA ubiquitination is required for cisplatin-induced FANCD2 monoubiquitylation by modifying a previously described approach (Niimi et al., >>2008<<). Cells were transfected with an siRNA that depletes endogenous PCNA along with plasmids that express siRNA-resistant wild-type PCNA (PCNAWT) or PCNA mutated at the ubiquitin acceptor site Lys164 (PCNAK164R). The depletion of endogenous
n2:mentions: n3:18845679

Subject Item: _:vb8944700
rdf:type: n2:Context
rdf:value: domains: the N terminus (amino acids 1–306) was predicted to contain three WD40 domains, and the C terminus (amino acids 307–375) was predicted to contain a zinc-binding region that is essential for E3 ligase activity (Meetei et al., >>2003<<). However, a very recent crystallographic structural analysis of Drosophila melanogaster FANCL has further refined our understanding of FANCL’s structure (Cole et al., 2010).
n2:mentions: n3:12973351

Subject Item: _:vb8944701
rdf:type: n2:Context
rdf:value: However, a very recent crystallographic structural analysis of Drosophila melanogaster FANCL has further refined our understanding of FANCL’s structure (Cole et al., >>2010<<). This study showed that the N terminus contains two separable domains, an E2-like fold (ELF) domain and a DRWD domain. To test which FANCL domain is important for PCNA binding, we examined binding to the entire N-terminal fragment (which
n2:mentions: n3:20154706

Subject Item: _:vb8944702
rdf:type: n2:Context
rdf:value: These observations, coupled with the fact that FANCL is recruited to chromatin after DNA damage (Matsushita et al., >>2005<<; Alpi et al., 2008), prompted us to ask whether PCNA ubiquitylation affected the binding of FANCL to chromatin.
n2:mentions: n3:16168378

Subject Item: _:vb8944703
rdf:type: n2:Context
rdf:value: These observations, coupled with the fact that FANCL is recruited to chromatin after DNA damage (Matsushita et al., 2005; Alpi et al., >>2008<<), prompted us to ask whether PCNA ubiquitylation affected the binding of FANCL to chromatin.
n2:mentions: n3:19111657

Subject Item: _:vb8944704
rdf:type: n2:Context
rdf:value: of FANCC, which encodes an FA core complex member, and RAD18 caused greater sensitivity to cisplatin than did either individual gene disruption alone, suggesting that the FA and RAD18 pathways are not epistatic (Hirano et al., >>2005<<). In contrast, our siRNA codepletion experiments suggest that the FA and RAD18 pathways may be epistatic in terms of cisplatin sensitivity (Fig.
n2:mentions: n3:15616572

Subject Item: _:vb8944705
rdf:type: n2:Context
rdf:value: However, it is worth noting that PCNA is still ubiquitylated in RAD18−/− cells and that cells expressing PCNAK164R are more sensitive to cisplatin than are RAD18−/− cells (Simpson et al., >>2006<<), thus raising the possibility that the lack of epistasis could be explained by the residual PCNA ubiquitylation in RAD18−/− cells.
n2:mentions: n3:16888649

Subject Item: _:vb8944706
rdf:type: n2:Context
rdf:value: Although previous studies suggest that ubiquitylated PCNA plays an important role in regulating the TLS polymerases REV1 and REV3 (Sarkar et al., >>2006<<; Shen et al., 2006), these results, taken in conjunction with the recent finding that FANCD2 has a PCNA interaction motif that is required for DNA damage–induced FANCD2 monoubiquitylation (Howlett et al., 2009), demonstrate that PCNA also
n2:mentions: n3:16482220

Subject Item: _:vb8944707
rdf:type: n2:Context
rdf:value: Although previous studies suggest that ubiquitylated PCNA plays an important role in regulating the TLS polymerases REV1 and REV3 (Sarkar et al., 2006; Shen et al., >>2006<<), these results, taken in conjunction with the recent finding that FANCD2 has a PCNA interaction motif that is required for DNA damage–induced FANCD2 monoubiquitylation (Howlett et al., 2009), demonstrate that PCNA also serves as a
n2:mentions: n3:16571727

Subject Item: _:vb8944708
rdf:type: n2:Context
rdf:value: and REV3 (Sarkar et al., 2006; Shen et al., 2006), these results, taken in conjunction with the recent finding that FANCD2 has a PCNA interaction motif that is required for DNA damage–induced FANCD2 monoubiquitylation (Howlett et al., >>2009<<), demonstrate that PCNA also serves as a central hub for the steps leading to the activation of the FA pathway in human cells.
n2:mentions: n3:19704162

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