ライフサイエンスコーパス: PTPH1

1 tivation of protein-tyrosine phosphatase H1 (PTPH1).

2 ate residue was changed to alanine (D811A in PTPH1).

3 ompared with catalytically inactive forms of PTPH1.

4 ytically active PTPH1 compared with inactive PTPH1.

5 duced the association between 14-3-3beta and PTPH1.

6 Thus the association between PTPH1 and 14-3-3beta is phosphorylation-dependent.

7 Furthermore, association of PTPH1 and 14-3-3beta was detected in several cell lines

8 as an adaptor molecule in the regulation of PTPH1 and may provide a link between serine/threonine an

9 Although both PTPH1 and Raf-1 form complexes with 14-3-3beta, they app

10 We present data that SHP-1 and PTPH1 are present in highly enriched protein fractions t

11 transfection assays indicated that SHP-1 and PTPH1 are the two principal PTPases capable of regulatin

12 itro and in vivo analyses further identified PTPH1 as a specific p38gamma phosphatase through PDZ-med

13 identified protein tyrosine phosphatase H1 (PTPH1) as a specific phosphatase for p38gamma mitogen-ac

14 Additional analyses showed that PTPH1 binds VDR and increases its cytoplasmic accumulati

15 n 14-3-3beta and various deletion mutants of PTPH1 by two-hybrid tests suggested that the integrity o

16 he presence of catalytically active forms of PTPH1 compared with catalytically inactive forms of PTPH

17 sed in cells expressing catalytically active PTPH1 compared with inactive PTPH1.

18 atase and suggest that PDZ-mediated p38gamma/PTPH1 complex may be a novel target for Ras-dependent ma

19 tyrosine 676 to phenylalanine (Y676F) in the PTPH1-D811A mutant led to a marked reduction in phosphot

20 The PTPH1-D811A mutant trapped primarily a 97-kDa tyrosine-p

21 horylation state of the TCR zeta ITAMs, with PTPH1 directly dephosphorylating zeta.

22 Ectopic expression of wild type PTPH1 dramatically inhibited cell growth, whereas a cata

23 To identify the direct target of PTPH1 in the cell, we generated a substrate-trapping mut

24 Binding of 14-3-3beta to PTPH1 in vitro was abolished by pretreating PTPH1 with p

25 n of the protein tyrosine phosphatase PTPN3 (PTPH1) in vitro and in living cells.

26 his is the first reported demonstration that PTPH1 is a candidate PTPase capable of interacting with

27 PTPH1 is a human protein-tyrosine phosphatase with homol

28 PTPN3 (PTPH1) is a cytoskeletal protein tyrosine phosphatase th

29 Protein-tyrosine phosphatase H1 (PTPH1) is a specific phosphatase of p38gamma mitogen-act

30 Additional experiments showed that PTPH1 itself plays a role in Ras-dependent malignant gro

31 g, and here, we show that p38gamma is also a PTPH1 kinase through which it executes its oncogenic act

32 Taken together, these results suggest that PTPH1 may be a negative regulator of TACE levels and fun

33 Our results suggest that PTPH1 may exert its effects on cell growth through depho

34 ling and is important for Ras, p38gamma, and PTPH1 oncogenic activity.

35 n and depletion of induced VDR abolishes the PTPH1 oncogenic activity.

36 Indeed, PTPH1 promotes breast cancer growth by a mechanism indep

37 Moreover, Ras increases both p38gamma and PTPH1 protein expression and there is a coupling of incr

38 here is a coupling of increased p38gamma and PTPH1 protein expression in primary colon cancer tissues

39 Moreover, induction of wild type PTPH1 resulted in specific dephosphorylation of VCP with

40 aled a novel stress pathway from p38gamma to PTPH1/Ser-459 phosphorylation in regulating cell growth

41 Silencing the p38gamma/c-Jun/PTPH1 signaling network increased sensitivities to TKIs

42 activity is regulated by the p38gamma/c-Jun/PTPH1 signaling network, whose disruption may be a novel

43 ere, we report that the tyrosine phosphatase PTPH1 stimulates breast cancer growth through regulating

44 Like wild type PTPH1, this double mutant also inhibited cell proliferat

45 is mediated via binding of the PDZ domain of PTPH1 to the COOH terminus of TACE.

46 PTPH1 was found to associate with 14-3-3beta using a yea

47 PTPH1 was identified as a substrate of p38gamma by unbia

48 and 4.1-related protein-tyrosine phosphatase PTPH1 was introduced into NIH3T3 cells under the control

49 PTPH1 was shown to be overexpressed in 49% of primary br

50 PTPH1 was the predominant phosphatase capable of complex

51 Two novel motifs RSLS359VE and RVDS853EP in PTPH1 were identified as major 14-3-3beta-binding sites,

52 report that the protein-tyrosine phosphatase PTPH1, which contains both a band 4.1 domain and a singl

53 PTPH1 in vitro was abolished by pretreating PTPH1 with potato acid phosphatase and was greatly enhan