ライフサイエンスコーパス: carboxypeptidase Y

1 not effect maturation of a vacuolar enzyme (carboxypeptidase Y).

2 thetic intermediate of the vacuolar protein, carboxypeptidase Y.

3 se of the trimer cone, become susceptible to carboxypeptidase Y.

4 loop truncation mutants could be removed by carboxypeptidase Y.

5 ell wall assembly, and delayed maturation of carboxypeptidase Y.

6 cysteine) and by C-terminal truncation using carboxypeptidase Y.

7 s that secreted strong-to-moderate levels of carboxypeptidase Y.

8 f Saccharomyces cerevisiae for missorting of carboxypeptidase Y.

9 ducts were then degraded to dipeptides using carboxypeptidase Y.

10 c reticulum and a block in the maturation of carboxypeptidase Y.

11 onversion to the readily detectable SL8 with carboxypeptidase Y.

12 mately 50% of the soluble vacuolar hydrolase carboxypeptidase Y.

13 n the Golgi to vacuole transport pathway for carboxypeptidase Y.

14 ibody-specific epitopes from intact cells by carboxypeptidase Y.

15 ential for delivery of the vacuolar protease carboxypeptidase Y.

16 d processing of the soluble vacuolar protein carboxypeptidase Y.

17 ecause no effect on the rate of transport of carboxypeptidase Y, a non-GPI-anchored protein, was obse

18 ants grow poorly under reductive stress, and carboxypeptidase Y activity is less than 10% of that in

19 ail of Ste13p, and also caused missorting of carboxypeptidase Y and accelerated vacuolar degradation

20 Vps67p, appeared to be involved in both the carboxypeptidase Y and alkaline phosphatase pathways.

21 along two distinct routes referred to as the carboxypeptidase Y and alkaline phosphatase pathways.

22 ells depleted for Tlg2p missort a portion of carboxypeptidase Y and are defective in endocytosis.

23 Finally, using misfolded yeast carboxypeptidase Y and chicken ovalbumin as glycoprotein

24 degrees C and display normal trafficking of carboxypeptidase Y and KKXX-tagged proteins at a permiss

25 asmic reticulum form) of the vacuolar enzyme carboxypeptidase Y and morphological abnormalities consi

26 o redirect the vacuolar destination of plant carboxypeptidase Y and other proteins in Arabidopsis sus

27 e vacuolar proteins alkaline phosphatase and carboxypeptidase Y and the vacuolar membrane H(+)-ATPase

28 which secretes the serine carboxypeptidase, carboxypeptidase Y, and other proteins normally targeted

29 51p (Vps21p), the resident vacuolar protease carboxypeptidase Y, and the vacuolar H+-ATPase Vph1p.

30 turation and sorting of the vacuolar protein carboxypeptidase Y as measures of protein sorting at the

31 missorting of 70% of the vacuolar hydrolase carboxypeptidase Y as well as the mislocalization of lat

32 ve in the maturation of the vacuolar protein carboxypeptidase Y, as well as in the secretion of inver

33 enzyme reduces proper folding of endogenous carboxypeptidase Y by about 40%.

34 inaris, LcL) with the carbohydrate moiety of carboxypeptidase Y (CaY) was studied using both atomic f

35 both GGA genes causes defects in sorting of carboxypeptidase Y (CPY) and proteinase A to the vacuole

36 omyces cerevisiae, vacuolar proteins such as carboxypeptidase Y (CPY) are actively sorted away from t

37 transport rate for an unglycosylated mutant carboxypeptidase Y (CPY) is markedly reduced.

38 sorting defect in which the vacuolar protein carboxypeptidase Y (CPY) is missorted and secreted from

39 he vacuole through a well defined route, the carboxypeptidase Y (CPY) pathway.

40 and secreted the soluble vacuolar hydrolase carboxypeptidase Y (CPY) rapidly and reversibly when vti

41 he sorting of the soluble vacuolar hydrolase carboxypeptidase Y (CPY) to the Saccharomyces cerevisiae

42 In addition, sorting of carboxypeptidase Y (CPY) to the vacuole was delayed, and

43 VE domain-containing proteins, which mediate carboxypeptidase Y (CPY) transport to the vacuole by the

44 Carboxypeptidase Y (CPY) travels through a prevacuolar/e

45 mutant, which lacks the sorting receptor for carboxypeptidase Y (CPY), accumulates both invertase and

46 hagy, whereas complex II is required for the carboxypeptidase Y (CPY)-to-vacuole pathway.

47 ERAD, we studied a new misfolded variant of carboxypeptidase Y (CPY).

48 can protect its s10 part against cleavage by carboxypeptidase Y (CPY).

49 detected between PDI and the ER precursor of carboxypeptidase Y (CPY).

50 hat measures transport-coupled maturation of carboxypeptidase Y (CPY).

51 d protein mimics zeolin or a mutated form of carboxypeptidase Y (CPY*) also induced autophagy in an I

52 In yeast, a mutant of carboxypeptidase Y (CPY*) was found to be a luminal ER s

53 d compare them with those for mutant form of carboxypeptidase Y (CPY*), a soluble luminal protein.

54 Zn2+ sensitivity and partially suppress the carboxypeptidase Y deficiency.

55 sequence of peptides by their digestion with carboxypeptidase Y directly on ProteinChip surfaces coup

56 of linear peptides from the ERAD substrate, carboxypeptidase Y G255R (CPY*), and binds a model unfol

57 had extensive similarity to the yeast serine carboxypeptidase Y gene.

58 e newly synthesized soluble vacuolar protein carboxypeptidase Y is missorted in nhx1 delta cells, and

59 essing and sorting of the vacuolar hydrolase carboxypeptidase Y is normal.

60 e-sensitive ero1-1 mutant, newly synthesized carboxypeptidase Y is retained in the ER and lacks disul

61 More than 95% of carboxypeptidase Y is secreted from these cells in its G

62 l in luv1 mutants, but some portion (28%) of carboxypeptidase Y is secreted.

63 aturation of isomerase-requiring substrates (carboxypeptidase Y) is impaired.

64 four carboxypeptidases, Arabidopsis thaliana carboxypeptidase Y-like protein, rice serine carboxypept

65 mperature were also found to have defects in carboxypeptidase Y maturation, giving emphasis to our pr

66 2p, Eug1p, Eps1p) are required for efficient carboxypeptidase Y maturation.

67 ps28 null mutant cells (approximately 40-50% carboxypeptidase Y missorted).

68 Gga function was studied using an assay for carboxypeptidase Y missorting and synthetic temperature-

69 The Kex2p mislocalization and carboxypeptidase Y missorting phenotypes were exhibited

70 idative protein folding of the model protein carboxypeptidase Y occurs with similar kinetics to the w

71 Although maturation of glycosylated carboxypeptidase Y occurs with wild-type kinetics in Del

72 Most surprisingly, Och1p can use either the carboxypeptidase Y or AP-3 pathways to reach the vacuole

73 hibited a significant defect in transport of carboxypeptidase Y or carboxypeptidase S to the vacuole

74 be released by trypsin treatment but not by carboxypeptidase Y or chymotrypsin treatment, we suggest

75 degrees C and accumulate the ER precursor of carboxypeptidase Y (p1 CPY).

76 vacuole was observed: transport via both the carboxypeptidase Y pathway and the alkaline phosphatase

77 ovel gene products were involved only in the carboxypeptidase Y pathway, whereas a few, including Mon

78 s and for proper protein sorting through the carboxypeptidase Y pathway.

79 on of CER1 slowed the folding of reduced pro-carboxypeptidase Y (pro-CPY) approximately twofold in ye

80 e Golgi-precursors of the soluble hydrolases carboxypeptidase Y, proteinase A, and proteinase B to th

81 Proper cycling of the carboxypeptidase Y receptor Vps10p between the TGN and p

82 ntial for endosome-to-Golgi retrieval of the carboxypeptidase Y receptor Vps10p.

83 mediates endosome-to-Golgi transport of the carboxypeptidase Y receptor Vps10p.

84 ase experiments monitoring the maturation of carboxypeptidase Y reveal that oxidative folding is grea

85 HX20 affected protein sorting as measured by carboxypeptidase Y secretion in yeast mutants grown at a

86 whole Arabidopsis seedlings also resulted in carboxypeptidase Y secretion, indicating that the drug h

87 The recycling of the carboxypeptidase Y sorting receptor, Vps10p, between the

88 Defects are seen in carboxypeptidase Y sorting, alkaline phosphatase transpo

89 the portion of the receptor responsible for carboxypeptidase Y sorting, is also coimmunoprecipitated

90 s the route that several proteins, including carboxypeptidase Y, take from the late Golgi to the vacu

91 No difference in carboxypeptidase Y targeting or processing is observed b

92 for the ERAD of CPY* (a misfolded version of carboxypeptidase Y that has five disulfide bonds).

93 ogy and defects related to the maturation of carboxypeptidase Y that is not dependent on the catalyti

94 ect in the transport of the vacuolar protein carboxypeptidase Y through the Golgi.

95 d results in a slight missorting of vacuolar carboxypeptidase Y to the cell surface.

96 n BET5 (bet5-1) that blocks the transport of carboxypeptidase Y to the vacuole and prevents secretion

97 Transport of carboxypeptidase Y to the vacuole is also perturbed, but

98 ane Golgi receptor responsible for targeting carboxypeptidase Y to the vacuole, causes the mutant hyb

99 ent alpha-factor maturation and transport of carboxypeptidase Y to the vacuole.

100 t for the delivery of the biosynthetic cargo carboxypeptidase Y to the vacuole.

101 in yeast resulted in impaired trafficking of carboxypeptidase Y to the vacuole.

102 ave colocalized antibodies against Ste2p and carboxypeptidase Y to this compartment, thereby identify

103 re-sensitive mutants of Vti1p show a similar carboxypeptidase Y trafficking defect, but the secretion

104 anisms; overexpressing VipA has an effect on carboxypeptidase Y trafficking, whereas VipD interferes

105 e in yeast causes defects in both growth and carboxypeptidase Y trafficking/processing.

106 omyces cerevisiae, vacuolar proteins such as carboxypeptidase Y transit from the Golgi to the lysosom

107 At semipermissive temperatures, carboxypeptidase Y transit time to the vacuole was slowe

108 e adaptor protein-1 complex, and Vps10p, the carboxypeptidase Y vacuolar protein receptor, are associ

109 nonpermissive temperature, newly synthesized carboxypeptidase Y was secreted, indicating that Vps9p f

110 osphatase, and a soluable vacuolar protease, carboxypeptidase Y. were also detected outside spores af

111 PA28 was inactivated by treatment with carboxypeptidase Y, which cleaved Tyr and Ile residues f

112 s for compounds that induce the secretion of carboxypeptidase Y, which is normally targeted to the va