ライフサイエンスコーパス: TAP2

1 ter associated with antigen processing (Tap1-Tap2).

2 ated with antigen processing genes (TAP1 and TAP2).

3 including LMP2 and LMP7 as well as TAP1 and TAP2.

4 air nucleotide binding relative to wild type TAP2.

5 n disulfide isomerase A3, tapasin, TAP1, and TAP2.

6 TAP transporter is a heterodimer of TAP1 and TAP2.

7 sociated with antigen processing 1 (TAP1) or TAP2.

8 including beta-2 microglobulin, (TAP1), and TAP2.

9 h recruits one MHC I molecule to TAP1 and/or TAP2.

10 ocated in the N-terminal domains of TAP1 and TAP2.

11 st the membrane-spanning regions of TAP1 and TAP2.

12 or peptide transporter genes TAP1 (0101) and TAP2 (0101) genes as well as tumor necrosis factor micro

13 HLA-DNA to RING3 (45 kb), as well as TAP1 to TAP2 (15 kb), by use of independent CEPH haplotypes indi

14 The results suggest that the permissive TAP2-A allele evolved in at least two steps, each partia

15 R, 5.56; 95% CI, 1.34-23.10; P=.018) and the TAP2 Ala665 (OR, 2.22; 95% CI, 1.28-3.84; P=.005) were a

16 TAP2 Ala665 was also associated with resistance (OR, 2.2

17 porter associated with antigen processing 2 (TAP2) allele were present at altered frequency in patien

18 the 25 residues by which the two functional TAP2 alleles differ, we have localized differential tran

19 Cotransfection of B78H1 with TAP2 and class I H chain genes is sufficient to reconsti

20 6F10 sublines, is also selectively devoid of TAP2 and low molecular weight protein 7 as well as class

21 Strikingly, nearby tap2 and MHC class I genes also retain ancient sequence

22 ectly target the peptide transporter subunit TAP2 and reduce levels of the TAP1 subunit, MHC class I

23 hich we have previously shown is an eQTL for TAP2 and significantly associated with fecundability (ti

24 of CD11c, CD40, CCR7 as well as LMP2, TAP1, TAP2 and tapasin than conv. mix-matured DC.

25 the dimerization interface between TAP1 and TAP2 and the tapasin docking sites for PLC assembly are

26 We show tapasin binding to both TAP1 and TAP2 and to the corresponding nucleotide binding domain-

27 e show that the physical interaction between TAP2 and TPN is disrupted by benzene, a compound known t

28 rphisms (SNPs) in 5 genes (LMP2, TAP1, LMP7, TAP2, and Tapasin) were investigated for association wit

29 ble APM components low-m.w. protein 2, TAP1, TAP2, and tapasin.

30 1) up-regulation of the APM components TAP1, TAP2, and tapasin.

31 ssociated with antigen processing (TAP)1 and TAP2, and the proteasomal components low molecular weigh

32 k of association between alleles of TAP1 and TAP2 (approximately 15 kb) has been observed, suggesting

33 unctional evidence that the NBDs of TAP1 and TAP2 are non-equivalent.

34 Here we show that both TAP1 and TAP2 are phosphorylated under physiological conditions.

35 Thus, the MSRs of both TAP1 and TAP2 are required for binding peptide.

36 Two subunits, TAP1 and TAP2, are necessary and sufficient for peptide binding a

37 Two subunits, TAP1 and TAP2, are required for peptide transport, and ATP hydrol

38 ressed alleles correspond to UAA adjacent to TAP2 as in domestic ducks, we cloned and sequenced genom

39 N-terminal domain TMD0 of mammalian TAP1 and TAP2 as well as avian TAP2 recruits tapasin.

40 erious because this interaction is lost upon TAP2 association.

41 en the UK control and patient groups, and in TAP2 between the Polish control and patient groups.

42 We detected significant differences in TAP2 between the UK control and patient groups, and in T

43 reveals previously unrecognized functions of TAP2 beyond antigen presentation and establishes a rever

44 cotransfection with genes encoding TAP1 and TAP2 but not individual TAP subunits, beta(2)m, or tapas

45 pidly, increasing 20-fold (TAP1) or 10-fold (TAP2) by 12 h, whereas HLA class I mRNA is induced more

46 In the rat, two alleles of the TAP2 chain differ in their permissiveness to the transpo

47 nged chimeras as well as to a truncated TAP1.TAP2 complex containing just the membrane-spanning regio

48 ucleotide binding at the TAP2 site upon TAP1/TAP2 complex formation.

49 The TAP1/TAP2 complex is required for peptide translocation acros

50 the role of each structural unit of the TAP1/TAP2 complex, we generated two chimeras containing TAP1

51 ly reduced efficiencies relative to the TAP1/TAP2 complex.

52 s stabilize the peptide binding site of TAP1.TAP2 complexes against inactivation, and enhanced thermo

53 her the two nucleotide-binding sites of TAP1/TAP2 complexes also differed in their nucleotide binding

54 The enhanced structural stability of TAP1.TAP2 complexes in the presence of tapasin might explain

55 eptide transport, and ATP hydrolysis by TAP1.TAP2 complexes is important for transport activity.

56 TAP1/TAP2 complexes translocate peptides from the cytosol to

57 ed for high affinity peptide binding to TAP1.TAP2 complexes, and in fact, the presence of tapasin sli

58 ding to a cytosol-accessible surface of TAP1/TAP2 complexes, but the location of the TAP peptide-bind

59 ions occurring on the cytosolic face of TAP1/TAP2 complexes, we investigated quaternary associations

60 nucleotide binding sites are present in TAP1.TAP2 complexes.

61 s with relatively similar affinities in TAP1/TAP2 complexes.

62 ranslocation are detectable with TAP1(K544M).TAP2 complexes.

63 TAP1 and TAP2 contain an N-terminal hydrophobic membrane-spanning

64 ed in peptide binding, such as TAP1-Val-288, TAP2-Cys-213, TAP2-Met-218.

65 observation that the Q10 hybrid assembly is TAP2-dependent supports the notion that Q10 groove is lo

66 associated with antigen processing TAP1 and TAP2, DMA and DMB which are involved in editing class II

67 The identical mutation in TAP2 does not significantly impair nucleotide binding re

68 ssing (TAP) comprises two subunits, TAP1 and TAP2, each containing a hydrophobic membrane-spanning re

69 onsists of two homologous subunits, TAP1 and TAP2, each of which contains an N-terminal domain (N-dom

70 transporter formed of two subunits, TAP1 and TAP2, each of which has an N-terminal membrane-spanning

71 gs with known anti-cancer activity increased TAP2 expression and its function in lung cancer cells.

72 sociation between the rs2071473 genotype and TAP2 expression by using GTEx data and demonstrated that

73 identification of compounds able to increase TAP2 expression in NSCLC cells.

74 Besides substantial reduction in TAP1 and TAP2 expression, peripheral blood mononuclear cells from

75 and L66) in the first and second TM helix of TAP2 form a functional unit acting as a docking site for

76 We found that avian and mammalian TAP1 and TAP2 form heterodimeric complexes across taxa.

77 c ducks, we cloned and sequenced genomic UAA-TAP2 fragments from all mallards, which matched transcri

78 Strikingly, however, only TAP1 and TAP2 from the same taxon can form a functional heterodim

79 DQB1 (6 cases), and an 8.8-kb segment of the TAP2 gene (3 cases).

80 sion of an alternative splice product of the Tap2 gene may contribute to broaden immune diversity, a

81 evels and the chromatin accessibility of the TAP2 gene promoter in NSCLC cells and reproduced all the

82 two patients we identified a mutation in the TAP2 gene responsible for the defective expression of th

83 rize a putative recombination hotspot in the TAP2 gene within the class II region of the MHC.

84 A-UEA The UAA gene, situated proximal to the TAP2 gene, is expressed at levels 10-fold greater than t

85 isted of a (TGGA)12 tandem repeat within the TAP2 gene.

86 nd nucleotide binding site, a glutamic acid (TAP2 Glu(632)) follows the Walker B motif, and the switc

87 regulation of 11 of these genes (MTCH2, ELL, TAP2, HDC, DMWD, MYCL, SLC4A9, ABCA7, CSTF1, PTK2B, and

88 TAP1 and TAP2, or of oligomerization of TAP1/TAP2 heterodimers on membranes.

89 and the switch region contains a histidine (TAP2 His(661)).

90 ty complex class I chain-related gene A, and TAP2 immunohistochemistry staining to assess cell surfac

91 cytes (TILs) and the APM components TAP1 and TAP2 in 819 baseline/pre-treatment NSCLCs from patients

92 examined the polymorphism in mouse TAP1 and TAP2 in inbred mice.

93 Silencing of TAP2 in lung cancer cells altered key intracellular immu

94 Differences between TAP1 and TAP2 in the nucleotide-binding site may be related to th

95 cept T1ctr interacts with wild type TAP1 and TAP2, indicating possibilities for homodimerization of T

96 No such effects were observed for the TAP1/TAP2 interaction or the complex formation between TPN an

97 The TAP heterodimer (TAP1-TAP2) introduces the final component of the MHC class I

98 Here, the first alternative splicing of Tap2 is described.

99 ion by using GTEx data and demonstrated that TAP2 is expressed by decidual stromal cells at the mater

100 photocrosslinking of 8-azido-ATP to TAP1 and TAP2 it seems that ICP47 does not prevent ATP from bindi

101 ptide translocation is undetectable for TAP1.TAP2(K509M) complexes, but low levels of translocation a

102 Mutants TAP1(K544M) and TAP2(K509M) were expressed in insect cells, and the effe

103 Treatment with IL-4 reduced TAP2 levels and the chromatin accessibility of the TAP2

104 the four genes encoded within the MHC (TAP1, TAP2, LMP2, and LMP7), as well as LMP10, which is encode

105 TAP2 loss in human NSCLCs was associated with reduced TA

106 eproduced all the functional consequences of TAP2 loss.

107 essential for peptide translocation but that TAP2-mediated ATP hydrolysis is critical, not only for t

108 associated with antigen processing (TAP1 and TAP2), members of the ABC transporter family that play a

109 binding, such as TAP1-Val-288, TAP2-Cys-213, TAP2-Met-218.

110 ntigen processing and presentation (TAP1 and TAP2, MHC class I and II, CD80), regulators of apoptosis

111 R primers to selectively amplify recombinant TAP2 molecules revealed a highly localized meiotic cross

112 Tap2iso mRNA was normally coexpressed with Tap2 mRNA in all human lymphocyte cell lines examined.

113 avy chain, beta2 microglobulin, and TAP1 and TAP2 mRNAs revealed increased expression in a majority o

114 containing TAP1 MSR and TAP2 NBD (T1MT2C) or TAP2 MSR and TAP1 NBD (T2MT1C).

115 nerated two chimeras containing TAP1 MSR and TAP2 NBD (T1MT2C) or TAP2 MSR and TAP1 NBD (T2MT1C).

116 as individual subunits or domains, TAP1 and TAP2 NBD differ markedly in their nucleotide binding pro

117 Thus, TAP1-TAP2 NBD dimers are not fully stabilized by nucleotides

118 ssibility of distinct functions for TAP1 and TAP2 NBD during a single translocation cycle.

119 TAP1/TAP2 NBD interactions appear to contribute at least in p

120 endogenous class Ia and Ib at the surface of TAP2-negative as well as TAP2-transfected B78H1 makes th

121 th TAP1 enhanced the binding affinity of the TAP2 nucleotide-binding site for both nucleotides.

122 dependent upon the presence of a functional TAP2 nucleotide-binding site.

123 ssibilities for homodimerization of TAP1 and TAP2, or of oligomerization of TAP1/TAP2 heterodimers on

124 These results indicate that RT1-linked Tap2 polymorphism in the rat strongly influences peptide

125 TAP is made up of the TAP1 and TAP2 polypeptides, which each possess a nucleotide bindi

126 s showed that H-RS cells were uniformly TAP1/TAP2-positive and expressed HLA class I in the majority

127 in human NSCLCs was associated with reduced TAP2 promoter chromatin accessibility and elevated IL-4

128 MHC-encoded transporter composed of TAP1 and TAP2 protein delivery.

129 We identified cancer cell selective TAP2 protein downregulation in 42.4% of treatment naive

130 TAP1 and TAP2 proteins are also induced rapidly, increasing 10-fo

131 The TAP1 and TAP2 proteins form a heterodimer that transports short p

132 of mammalian TAP1 and TAP2 as well as avian TAP2 recruits tapasin.

133 rker was derived for each endotype; BPGM and TAP2 reliably identified patients with a Mars1 endotype.

134 mutagenesis to identify the residues in rat TAP2 responsible for differential transport between the

135 In contrast, less than 5% of the Kb within TAP2-RMA-S microsomes associated with the remaining TAP1

136 ination frequency and haplotype diversity in TAP2 showed that linkage disequilibrium measures were a

137 that alterations at Glu(632) and His(661) of TAP2 significantly reduced peptide translocation and/or

138 n part to enhanced nucleotide binding at the TAP2 site upon TAP1/TAP2 complex formation.

139 ity, the second nucleotide binding site (the TAP2 site) appears to be the main site driving peptide t

140 d from differential labeling of the TAP1 and TAP2 subunits using sICP47 fragments with chemical cross

141 For these studies, we tagged the TAP1 and TAP2 subunits with enhanced cyan fluorescent protein and

142 eotide-binding domains (NBD) in the TAP1 and TAP2 subunits.

143 residues in the Walker A motifs of TAP1 and TAP2 suggests that TAP1-mediated ATP hydrolysis is not e

144 cation efficiency of TAP1/T2MT1C relative to TAP2/T1MT2C complexes correlates with enhanced binding o

145 d complexes, T1MT2C/T2MT1C, TAP1/T2MT1C, and TAP2/T1MT2C, all translocate peptides, but with progress

146 We show that TAP1/T2MT1C, TAP2/T1MT2C, and T1MT2C/T2MT1C complexes bind peptide wi

147 2-748) and two C-terminal fragments of human TAP2 (T2c, residues 399-686 and T2ctr, residues 433-686)

148 By contrast, TAP1/T1MT2C and TAP2/T2MT1C complexes, although observed, are impaired f

149 ular weight TAP complexes that contain TAP1, TAP2, tapasin, and class I heterodimers.

150 ed with antigen-processing subunits TAP1 and TAP2 that were altered at the conserved lysine residue i

151 two structurally related subunits, TAP1 and TAP2, that form stable complexes in endoplasmic reticulu

152 9 and the antigen transporter genes Tap1 and Tap2 The PSMB8 inhibitor ONX-0914 reversed the effects o

153 PLC resulting in greater significance of the TAP2/TPN interaction for MHC loading.

154 b at the surface of TAP2-negative as well as TAP2-transfected B78H1 makes this system a suitable mode

155 potential in syngeneic B6 mice compared with TAP2-transfected parental melanoma.

156 ed with peptide transport by the MHC-encoded Tap2 transporter, on the function of HLA-B27 as a restri

157 class I genes in the complex, arranged TAP1-TAP2-UAA-UBA-UCA-UDA-UEA The UAA gene, situated proximal

158 amma-(32)P]ATP and 8-azido-[alpha-(32)P]ADP, TAP2 was found to have reduced affinity for nucleotides

159 ed with antigen processing (TAP) loci (TAP1, TAP2) were investigated in 100 members of 16 families wi

160 sociation of two half-transporters, TAP1 and TAP2, with a typical ABC transporter core that consists