ライフサイエンスコーパス: FANCE

1 FANCE, a subunit of the FA core complex, plays an essent

2 NCE (FANCE-T346A/S374A), when expressed in a FANCE-deficient cell line, allows FANCD2 monoubiquitinat

3 FANCC and FANCE act as substrate receptors and restrict monoubiqui

4 The recent cloning of the FANCF and FANCE genes has allowed us to investigate the interactio

5 gnaling, leading to defective Chk1, p53, and FANCE phosphorylation; 53BP1 focus formation; and Cdc25A

6 ecause FANCE and FANCC interact in vitro and FANCE is required for FANCD2 monoubiquitination, we reas

7 FANCE-deficient cells to a similar degree as FANCE null cells, suggesting the significance of the FAN

8 Because FANCE and FANCC interact in vitro and FANCE is required

9 The FA proteins FANCA, FANCC, FANCE, FANCF, FANCG, and FANCL participate in a core com

10 ia-associated proteins (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG and FANCL) form a nuclear Fanconi an

11 d with Fanconi anemia (FANCA, FANCC, FANCD2, FANCE, FANCF and FANCG) as well as BRCA1 and BRCA2 (FANC

12 anemia gene products (FANCA, FANCC, FANCD2, FANCE, FANCF, and FANCG proteins) interact in a common p

13 ding at least 6 genes (FANCA, FANCC, FANCD2, FANCE, FANCF, and FANCG).

14 genes (FANCA, FANCB, FANCC, FANCD1, FANCD2, FANCE, FANCF, FANCG, and FANCL), and identified ortholog

15 groups (FANCA, FANCB, FANCC, FANCD1, FANCD2, FANCE, FANCF, FANCG, FANCI, FANCJ, FANCL, FANCM, and FAN

16 A nonphosphorylated mutant form of FANCE (FANCE-T346A/S374A), when expressed in a FANCE-deficient

17 ystallographic and biological study of human FANCE.

18 hese findings show that the newly identified FANCE protein is an integral part of the FA pathway, and

19 Here we show that the recently identified FANCE protein is part of this nuclear complex, binding b

20 Indeed, FANCE is required for the nuclear accumulation of FANCC

21 However, the mutant FANCE protein fails to complement the mitomycin C hypers

22 A nonphosphorylated mutant form of FANCE (FANCE-T346A/S374A), when expressed in a FANCE-def

23 FANCC with FANCE and a weaker interaction of FANCE with both FANCA and FANCG.

24 Chk1-mediated phosphorylation of FANCE is required for a function independent of FANCD2 m

25 The portion of FANCE defined by our crystallographic analysis is suffic

26 Phosphorylated FANCE assembles in nuclear foci and colocalizes with FAN

27 ferred cellular sensitivity in reconstituted FANCE-deficient cells to a similar degree as FANCE null

28 Hemagglutinin (HA)-tagged FANCE protein localizes diffusely in the nucleus.

29 In normal cells, HA-tagged FANCE protein coimmunoprecipitates with FANCA, FANCC, an

30 Our data indicate that FANCE is a component of the nuclear FA complex in vivo a

31 FANCD2 monoubiquitination, we reasoned that FANCE is a component of the FA complex in vivo.

32 The FANCE protein plays an essential role in the FA process

33 Disease-associated mutations disrupt the FANCE-FANCD2 interaction, providing structural insight i

34 FANCE mutant that specifically disrupts the FANCE-FANCD2 interaction as a tool, we found that the in

35 Intriguingly, ectopic expression of the FANCE C terminus fragment alone in FA normal cells disru

36 ll cells, suggesting the significance of the FANCE-FANCD2 interaction in promoting cisplatin resistan

37 repair, consolidating the importance of the FANCE-FANCD2 interaction in the DNA cross-link repair.

38 DNA damage, Chk1 directly phosphorylates the FANCE subunit of the FA core complex on two conserved si

39 Using the FANCE mutant that specifically disrupts the FANCE-FANCD2

40 nconi anemia subtype E (FA-E) cells with the FANCE cDNA restores the nuclear accumulation of FANCC pr

41 ease-associated FANCC mutants do not bind to FANCE, cannot accumulate in the nucleus and are unable t

42 teraction of FANCF with FANCG, of FANCC with FANCE and a weaker interaction of FANCE with both FANCA

43 ly, we analyzed a series of mutations within FANCE.