ライフサイエンスコーパス: CUG-BP

1 CUG-BP and ETR-3 like factor (CELF) proteins are regulat

2 CUG-BP and ETR-3-like factor proteins control developmen

3 CUG-BP was found to bind to the human cardiac troponin T

4 CUG-BP, ETR-3, and CELF4 are more broadly expressed, and

5 reening of a mouse liver cDNA library with a CUG-BP probe identified two mETR-3 cDNAs.

6 Although CUG-BP in nuclear extracts preferentially photocrosslink

7 ediated down-regulation of MBNL1, MBNL2, and CUG-BP in DM1 myoblasts demonstrated that MBNL1 plays a

8 The relative importance of MBNL1, MBNL2, and CUG-BP in DM1 pathogenesis is, however, unclear.

9 Both CUG-BP and mETR-3 bind to mETR-3 mRNA via CUG repeats, s

10 of genes regulated posttranscriptionally by CUG-BP therefore may contribute to DM pathogenesis.

11 is predicted to encode a member of the CELF (CUG-BP- and ETR-3-like factors) family of RNA-binding pr

12 cting regulators PTB, Fox, Muscleblind, CELF/CUG-BP, TIA-1 and hnRNP F/H, respectively.

13 This family, which we call CELF proteins for CUG-BP- and ETR-3-like factors, specifically bound MSE-c

14 t region in Mt-PK mRNA is a binding site for CUG-BP/hNab50 in vivo, and triplet repeat expansion lead

15 lear concentration of the hypophosphorylated CUG-BP/hNab50 isoform is increased in DMPK knockout mice

16 Moreover, CUG-BP localized to the base of the RNA hairpin and not

17 elevation of the hypophosphorylated form of CUG-BP/hNab50.

18 eats, suggesting the possible involvement of CUG-BP-like proteins in the regulation of mETR-3 process

19 Steady-state levels of CUG-BP, a regulator of pre-mRNA splicing proposed to med

20 0, thus facilitating nuclear localization of CUG-BP/hNab50.

21 ed in DM1 skeletal muscle; overexpression of CUG-BP in normal cells induces a switch to IR-A.

22 of MBNL1 and MBNL2 or the overexpression of CUG-BP in normal myoblasts results in abnormal IR splici

23 the key event, whereas the overexpression of CUG-BP plays a secondary role in the aberrant alternativ

24 in nuclear foci, the localization pattern of CUG-BP in both normal and DM cells was similar.

25 DMPK-mediated phosphorylation of CUG-BP/hNab50 results in dramatic reduction of the CUG-B

26 r distribution and RNA-binding properties of CUG-BP.

27 ld be, in part, a result of sequestration of CUG-BP/hNab50 and, in part, of lowered DMPK levels, whic

28 f DMPK could alter phosphorylation status of CUG-BP/hNab50, thus facilitating nuclear localization of

29 DMPK also interacts with and phosphorylates CUG-BP/hNab50 protein in vitro.

30 also demonstrated that CUG-binding protein (CUG-BP) binds a conserved CUG motif within a human cTNT

31 ion, elevated levels of CUG-binding protein (CUG-BP) have been shown to result in altered IR splicing

32 the binding of purified CUG-binding protein (CUG-BP) to these RNAs.

33 lear ribonucleoprotein, CUG-binding protein (CUG-BP), may mediate the trans-dominant effect of the RN

34 inding protein, identical to hNab50 protein (CUG-BP/hNab50), are altered in homozygous DM patient and

35 The novel protein, CUG-BP, is particularly interesting since it binds to tr

36 of the members of the CUG-binding proteins, CUG-BP, has been identified previously.

37 ated the role of three RNA-binding proteins, CUG-BP, hnRNP C and MBNL, as possible sequestered factor

38 th specific binding to CUG repeat sequences (CUG-BP/hNab50) that possibly plays a role in mRNA proces

39 re altered in homozygous DM patient and that CUG-BP/hNab50 is a substrate for DMPK both in vivo and i

40 g/photocrosslinking studies demonstrate that CUG-BP/hNab50 binds to RNAs containing the Mt-PK 3'-UTR.

41 Here we report that CUG-BP is one of a novel family of developmentally regul

42 escent protein (GFP) tags we have shown that CUG-BP and hnRNP C do not co-localise with expanded repe

43 We have shown that CUG-BP levels are elevated in DM1 cells by mechanisms th

44 ms an RNA hairpin structure and suggest that CUG-BP is unlikely to be a sequestered factor.

45 Our results suggest that CUG-BP regulates the equilibrium of splice site selectio

46 The CUG-BP and ETR-3 like factors (CELF) are a family of six

47 The CUG-BP protein mediates this switch through an intronic

48 The CUG-BP, Elav-like family (CELF) of RNA-binding proteins

49 The CUG-BP/hNab50 protein is localized predominantly in the

50 Furthermore, the CUG-BP exhibited no binding to an RNA oligonucleotide of

51 Members of the CUG-BP and ETR-3 like factor (CELF) protein family bind

52 Members of the CUG-BP, Elav-like family (CELF) regulate alternative spl

53 lation and intracellular localization of the CUG-BP/hNab50 protein.

54 These domains have common features with the CUG-BP and ETR3-like Factor (CELF) family of splicing re

55 kDa and displays a high level of homology to CUG-BP protein.

56 the ETR-3 molecule is similar to one within CUG-BP.