ライフサイエンスコーパス: PABP1

1 PABP1 has been proposed to participate at various steps

2 PABP1 relocalization was sharply decreased in cells infe

3 Here we show that poly(A)-binding protein 1 (PABP1) binds preferentially to INS-1 within the p17(gag)

4 r localization of poly(A)-binding protein 1 (PABP1) by indirect immunofluorescence as well as by tagg

5 d CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as

6 l protein, RPS17, poly(A)-binding protein 1 (PABP1), and the elongation factors, eEF1A and eEF2.

7 ludes cytoplasmic poly(A) binding protein 1 (PABP1).

8 nonhistone (polyadenylate-binding protein 1, PABP1) substrates induced by coactivator-associated argi

9 included RNA metabolism proteins hnRNPA1 and PABP1 and the glycolysis enzyme GAPDH.

10 starvation-induced PABP1-SIRT1 association, PABP1 deacetylation, and poly(A)RNA nuclear retention.

11 nuclear proteins revealed costaining between PABP1 and markers of nuclear speckles.

12 In the low expressing cells, PABP1 was localized in the cytoplasm, whereas in the hig

13 This establishes a new role for the cellular PABP1 inhibitor Paip2 as an innate defense that restrict

14 In contrast, PABP1 mRNA expression is minimal in oocytes and early em

15 ation, SIRT1 interacts with and deacetylates PABP1 and deactivates its poly(A)RNA binding, leading to

16 ing protein 2, which is known to destabilize PABP1 binding to poly(A) and inhibit steady-state transl

17 ng that active transcription is required for PABP1 export.

18 These results suggest a role for PABP1 in the inhibition of gag expression mediated throu

19 Consistent with roles for PABP1 and eIF2alpha in the pioneer round of translation,

20 However, CARM1 methylates histone H3, PABP1, AIB1, and a number of splicing factors, which str

21 similarity to the entire 5' UTR of the human PABP1 mRNA, but there is no similarity upstream of the t

22 of the transcription start site of the human PABP1 mRNA, indicating that the Pabp2 gene lacks 5' flan

23 it illustrates how a stress-induced rise in PABP1 triggered by virus infection can counter and surpa

24 synthesis and replication without increasing PABP1.

25 on is required for energy starvation-induced PABP1-SIRT1 association, PABP1 deacetylation, and poly(A

26 Second, mRNAs encoding somatic PABP isoform, PABP1, are present at high levels in meiotic and haploid

27 localize efficiently with Vif(IIIB) and mRNA-PABP1 complexes in stress granules in a manner that is p

28 3F imply that it occurs associated with mRNA-PABP1 in translationally active polysomes and to a lesse

29 Nuclear PABP1 observed either after overexpression or after tran

30 The ability of PABP1 to shuttle between nucleus and cytoplasm was also

31 binding, leading to nuclear accumulation of PABP1 and poly(A)RNA and thus facilitating eukaryotic ce

32 Accumulation of PABP1 in the nuclei was observed upon transcription inhi

33 ent cell lines and found that the binding of PABP1 to INS-1 RNA is significantly diminished in glial

34 We found that Unr stimulated the binding of PABP1 to mRNA, and that Unr was required for the stable

35 gag correlate with the absence of binding of PABP1 to the INS-1 RNA in cellular extracts.

36 olymers demonstrated preferential binding of PABP1 to the INS-1-containing RNA.

37 Coordinate control of PABP1, Paip2, and EDD1 required the virus-encoded UL38 m

38 The nuclear import of PABP1 is an energy-dependent process since PABP1 fails t

39 ll lines with EZM2302 leads to inhibition of PABP1 and SMB methylation and cell stasis with IC50 valu

40 r was required for the stable interaction of PABP1 and eIF4G in cells.

41 Our results suggest involvement of PABP1 in nuclear events associated with the formation an

42 populations producing physiologic levels of PABP1 and increased in cells with reduced levels of PABP

43 of cells producing high versus low levels of PABP1, we found that the percentage of RVFV N-positive c

44 nd increased in cells with reduced levels of PABP1.

45 mutagenesis showed that the minimal part of PABP1 retaining the ability to shuttle consists of the f

46 cells demonstrated a gross relocalization of PABP1 to the nucleus late in infection.

47 Here, we investigated the role of PABP1 during RVFV infection of HeLa cells.

48 ing RVFV infection leads to sequestration of PABP1 in the nuclear speckles, creating a state within t

49 Transfection of PABP1 or PABP1-GFP resulted in heterogeneity of intracel

50 Transfection of PABP1 or PABP1-GFP resulted in heterogeneity of intracellular dis

51 ity of polyadenylate-binding protein PABPC1 (PABP1) to stimulate translation is regulated by its repr

52 lacks 5' flanking sequences of the parental PABP1 gene.

53 was dependent on PABP accrual, as preventing PABP1 accumulation suppressed viral replication and inhi

54 n CARM1 substrates, poly(A)-binding protein (PABP1) and the transcriptional cofactor p300, was abolis

55 lasmic somatic cell poly(A)-binding protein (PABP1) is not expressed until later in embryogenesis.

56 via deacetylating a poly(A)-binding protein, PABP1.

57 Since PABP1 binds to all polyadenylated mRNAs, and is involved

58 f PABP1 is an energy-dependent process since PABP1 fails to enter the nucleus upon ATP depletion and

59 In addition, the SIRT1-PABP1 association is not specific to energy starvation b

60 th small interfering RNAs (siRNAs) targeting PABP1.

61 changed by siRNA treatment, indicating that PABP1 was not required for RVFV infection.

62 We show that PABP1 is able to enter the nucleus.

63 that the Pabp2 promoter is derived from the PABP1 5' UTR.

64 y 330 bases downstream of the capsite of the PABP1 mRNA, indicating that the Pabp2 promoter is derive

65 To determine whether PABP1 was required for RVFV infection, we measured the p

66 2 synthesis, stability, and association with PABP1.

67 ts ability to bind RNA, and to interact with PABP1.

68 hibits 72% identity to mammalian and Xenopus PABP1 and is the predominant poly(A)-binding protein exp