ライフサイエンスコーパス: ZO-2

1 ne encoding the tight junction protein TJP2 (ZO-2).

2 bound on the cytoplasmic surface to ZO-1 and ZO-2.

3 r exportation and proteosomal degradation of ZO-2.

4 de the cell polarity proteins Dlg1, PATJ and ZO-2.

5 junction proteins Claudin-1, Claudin-7, and ZO-2.

6 sary for interaction with the PDZ2 domain of ZO-2.

7 tight junction proteins, occludin, ZO-1, and ZO-2.

8 enuated 3-NC-induced hyperphosphorylation of ZO-2.

9 hionine-labeled in vitro translated ZO-1 and ZO-2.

10 interacted with in vitro translated ZO-1 and ZO-2.

11 xons 19-21 of 4.1R and residues 1054-1118 of ZO-2.

12 iously identified to interact with Cx43, and ZO-2, a potential novel interacting partner.

13 epithelial permeability via association with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and control

14 , in addition to tyrosine phosphorylation of ZO-2, also stimulates threonine phosphorylation of ZO-1

15 lular PDZ proteins, including MUPP1, MAGI-1, ZO-2 and Dlg1.

16 ed the expression of Cdx2 and Oct-4, but not ZO-2 and F-actin.

17 e report that JAM-A associates directly with ZO-2 and indirectly with afadin, and this complex, along

18 CH is accompanied by decreased expression of ZO-2 and nuclear expression of YAP.

19 4.1R is colocalized with ZO-2 and occludin at Madin-Darby canine kidney (MDCK) ce

20 nd in vivo binding assays indicate that both ZO-2 and occludin interact with specific domains within

21 ther of ZO-1, or one of the related proteins ZO-2 and ZO-3 (ZO proteins), or all three together.

22 ssumed that ZO-1, together with its homologs ZO-2 and ZO-3, serves as a platform to scaffold various

23 rks distinct from those of heterodimers with ZO-2 and ZO-3.

24 reviously, ZO-1 also forms heterodimers with ZO-2 and ZO-3.

25 on protein 2 (encoded by TJP2, also known as ZO-2) and bile acid Coenzyme A: amino acid N-acyltransfe

26 n-1, claudin-5, zonula occludens (ZO)-1, and ZO-2, and a TJ accessory protein annexin-ll.

27 of the TJ proteins, zonula occludens (ZO)-1, ZO-2, and cingulin, examination of the Triton X-100 solu

28 rmine tissue distribution of occludin, ZO-1, ZO-2, and claudin-1 in the rat cornea.

29 o Ser/Thr phosphorylation of occludin, ZO-1, ZO-2, and claudin-5.

30 PDZ proteins, including MUPP1, PATJ, MAGI-1, ZO-2, and Dlg1.

31 din, a second tight junction-specific MAGUK, ZO-2, and F-actin, although the nature and functional si

32 of Ad9 E4- ORF1 and the first PDZ domain of ZO-2, and in cells this interaction resulted in aberrant

33 Synaptojanin 1, PAK2, ZO-2, and TAFII70, which contain CIN85 SH3 recognition c

34 e for cytoplasmic proteins, presumably ZO-1, ZO-2, and ZO-3, in localizing occludin in tight junction

35 rier through disruption of TJs, and ZO-1 and ZO-2 are targets for the induction.

36 AmotL1 and ZO-2 are two candidates that could be harnessed to contr

37 Our results reveal a novel role of ZO-2 as a modulator of cell size.

38 We examined Cx43 interaction with ZO-1 and ZO-2 at different stages of the cell cycle and found tha

39 ilized ZO-2 suggest the presence of multiple ZO-2 binding sites in this domain.

40 ssed 4.1R containing the spectrin/actin- and ZO-2-binding domains was recruited to tight junctions in

41 Occludin, ZO-1, and ZO-2, but not claudin-1, are components of corneal epith

42 -2 in cells, and overexpression of wild-type ZO-2, but not mutant ZO-2 lacking the second and third P

43 ial cells than the up-regulation of ZO-1 and ZO-2 by itself.

44 rescence studies indicate that both ZO-1 and ZO-2 can co-localize with Cx43 within the plasma membran

45 Far Western analysis revealed that ZO-2 can directly bind to Cx43 independent of other inte

46 cause other tight junction components, ZO-1, ZO-2, cingulin, and the adherens junction protein E-cadh

47 distribution of TJ proteins (occludin, ZO-1, ZO-2, claudin-5) by CCL2.

48 lted in a decrease in the levels of ZO-1 and ZO-2 compared with untreated cells.

49 Co-immunoprecipitation of this domain with ZO-2 demonstrated preservation of the specificity of the

50 ZO-2 departure from the nucleus requires intact S257, an

51 xin exposure did not induce translocation of ZO-2, dephosphorylation or translocation of occludin, or

52 lts show that double knockdown (dKD) of ZO-1/ZO-2 elevates the apical epithelial tension and effectiv

53 ibits pro-apoptotic function of YAP, whereas ZO-2 enhances it.

54 This phosphorylation induces ZO-2 entry into the nucleus and accumulation in speckles

55 ZO-2 expression demonstrated a direct correlation with i

56 onclude that claudin-1, claudin-5, ZO-1, and ZO-2 expression exhibit differential developmental regul

57 ZO-2 expression was 45% and 70% lower (P<0.01) in the pl

58 IL-15-mediated up-regulation of ZO-1 and ZO-2 expression was independent of the IL-2Rbeta subunit

59 ocorticoids are associated with increases in ZO-2 expression, but not with occludin, claudin-1, claud

60 We report here that AmotL1 and ZO-2 form a tripartite complex with YAP and regulate its

61 leled by dissociation of occludin, ZO-1, and ZO-2 from the lateral TJ membrane without influencing th

62 that in confluent cultures newly synthesized ZO-2 goes directly to the plasma membrane.

63 Zona occludens 2 (ZO-2) has a dual localization.

64 pressed the TJ proteins claudin-5, ZO-1, and ZO-2; HIV-1 decreased TJ proteins expression and induced

65 ted impaired binding to and sequestration of ZO-2 in cells, and overexpression of wild-type ZO-2, but

66 However, further depletion of ZO-2 in Eph4 ZO-1KO cells, which do not express ZO-3, ca

67 iminishes expression of claudin-5, ZO-1, and ZO-2 in HBMECs.

68 showed an increase in the amount of ZO-1 and ZO-2 in high density fractions following ATP depletion,

69 f TJ-associated proteins occludin, ZO-1, and ZO-2 in LPS-treated THCE cells.

70 mely, occludin, zonula occludens (ZO)-1, and ZO-2 in the caveolar fraction of HBMECs.

71 enous glucocorticoids regulate claudin-5 and ZO-2 in vivo at some, but not all ages, and increases in

72 for interaction with ZO-1 during G0, whereas ZO-2 interaction occurred approximately equally during G

73 ins, hyperphosphorylated occludin, ZO-1, and ZO-2 into the tight junctional protein complex.

74 These results show that ZO-2 is implicated in regulating the nuclear shuttling o

75 with the candidate tumor suppressor protein ZO-2 is key to defining the unique transforming and tumo

76 At the plasma membrane ZO-2 is not O-GlcNAc, and instead, as TJs mature, it bec

77 In confluent epithelia, ZO-2 is present at tight junctions (TJs), whereas in spa

78 the tight junction protein zona occludens 2 (ZO-2 KD) induces cell hypertrophy by two mechanisms: pro

79 ZO-2 knockdown did not replicate either the permeability

80 expression of wild-type ZO-2, but not mutant ZO-2 lacking the second and third PDZ domains, interfere

81 Reduction of the ZO-2 level was associated with the disappearance of ZO-2

82 ecture to develop, as cells transfected with ZO-2 mutant S257A or S257E form aberrant cysts with mult

83 ed domains critical for the interaction with ZO-2, occludin, and F-actin.

84 entified by the rescue experiment with tjp-2/ZO-2 or the PAR complex (par-3, par-6, and prkci/atypica

85 meability, suggesting a relationship between ZO-2 phosphorylation and tight junction permeability.

86 ing motif to interact with zona occludens-2 (ZO-2) protein, which promotes YAP's translocation to the

87 Only depletion of ZO-2 reduced the nuclear import of YAP.

88 hat sustain the interaction between 4.1R and ZO-2 reside within the amino acids encoded by exons 19-2

89 We also asked if AmotL1, YAP and ZO-2 signal together.

90 vel was associated with the disappearance of ZO-2 staining from cell borders in 6-hour LPS-treated ce

91 nction, and binding studies with immobilized ZO-2 suggest the presence of multiple ZO-2 binding sites

92 eal novel posttranslational modifications of ZO-2 that regulate the intracellular fate of this protei

93 tro (along with claudins, occludin, ZO-1 and ZO-2), the tight junctional networks that form were disc

94 vities are required for membrane assembly of ZO-2 TJ protein, while only PKCzeta activity is involved

95 d that in sparse cultures, newly synthesized ZO-2 travels to the nucleus before reaching the plasma m

96 o AA or 15(S)-HETE led to Src-Pyk2-dependent ZO-2 tyrosine phosphorylation, tight junction disruption

97 ZO-2 was higher at 90% gestation, in newborn and adult s

98 examethasone than placebo-treated lambs, and ZO-2 was higher in fetuses of dexamethasone than placebo

99 Occludin, ZO-1, and ZO-2 were found at the cell borders of the superficial l

100 f endogenous ZO-1 and another family member, ZO-2, were disrupted.

101 otein kinase 1, which in turn phosphorylates ZO-2, which contains 16 SR repeats.

102 here that the PDZ domain-containing protein ZO-2, which is a candidate tumor suppressor protein, is

103 and activity, whereas depletion of ZO-1 and ZO-2, which is associated with reduced ZO-3 expression,

104 We confirmed the interaction of ZO-2 with Cx43 by using a combination of fusion protein

105 fically bind and sequester MUPP1, MAGI-1 and ZO-2 within insoluble complexes whereas trimers specific

106 action resulted in aberrant sequestration of ZO-2 within the cytoplasm.

107 oteins that organize tight junctions such as ZO-2, ZO-1, and occludin.

108 also bind to the scaffolding proteins ZO-1, ZO-2, ZO-3, cingulin, the membrane trafficking protein V

109 0 kDa specifically interact with the protein ZO-2 (zonula occludens-2).