ライフサイエンスコーパス: PtdIns3P

1 PtdIns3P 4-K is not the recently described "PIP5KIIalpha

2 PtdIns3P may play a role in modulating the Rab5 EEA1 int

3 calizes to early endocytic compartments in a PtdIns3P-dependent manner and modulates endosomal traffi

4 The stimulation of a PtdIns3P 5-OH kinase-catalysed synthesis of PtdIns(3,5)P

5 ) by a process that involves activation of a PtdIns3P 5-OH kinase.

6 s, PI3K-C2alpha regulates the formation of a PtdIns3P pool at the PRE required for Rab11 and Shh path

7 Substitution of the His residues abolishes PtdIns3P binding by the FYVE domain in vitro and in vivo

8 After aggregation, PtdIns3P 4-K calpain-dependently loses its susceptibilit

9 Prior to aggregation, PtdIns3P 4-K can be regulated negatively by the beta gam

10 ivities of phosphatidylinositol 3-kinase and PtdIns3P 4-K increase after aggregation.

11 In addition, PtdIns(4,5)P2 and PtdIns3P have been implicated in exocytosis and membrane

12 Another PtdIns3P-binding module, the PX domain of Vam7 and p40ph

13 pellers that bind polyphosphoinositides) are PtdIns3P and PtdIns(3,5)P2 binding autophagy related pro

14 e suggested that all Fab1p homologues may be PtdIns3P 5-kinases involved in membrane trafficking.

15 N family members Atg18, Atg21, and Hsv2 bind PtdIns3P and PtdIns(3,5)P2 with high affinities in the n

16 is requires the ability of Protrudin to bind PtdIns3P.

17 noncanonical lipid binding pocket that binds PtdIns3P.

18 -phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with

19 nd that the FYVE domain is critical for both PtdIns3P and Rab5 binding.

20 y and activation is highly dependent on both PtdIns3P-p40(phox) and Rac2-p67(phox) interactions and d

21 tion of PtdIns3P and then phosphorylation by PtdIns3P 4-kinase (PtdIns3P 4-K), a novel pathway appare

22 on of PtdIns(3,4)P2, the latter primarily by PtdIns3P 4-kinase.

23 tors, and the phosphorylation of PtdIns3P by PtdIns3P 4-kinase.

24 Loss of PI3K-C2alpha-derived PtdIns3P leads to mislocalization of PRE markers such as

25 Furthermore, it is shown that endosomal PtdIns3P/PtdIns(3,5)P2 is necessary for transferrin rece

26 Lowering the cytosolic pH enhances PtdIns3P affinity of the FYVE domain, reinforcing the an

27 he sn1 position in vitro making it the first PtdIns3P-specific phospholipase A1 (PLA1).

28 cessive protonation of which is required for PtdIns3P head group recognition as revealed by NMR.

29 sponse to platelet agonists, do not generate PtdIns3P or activate HsC2-PI3K under conditions that sti

30 ate (PtdIns3P) and cleaves the fatty acid in PtdIns3P at the sn1 position in vitro making it the firs

31 pression and, in turn, decreased PRR-induced PtdIns3P and autophagy and increased PRR-induced caspase

32 ression of ABH in vivo reduces intracellular PtdIns3P levels and its PtdIns3P-specific PLA1 activity

33 educes intracellular PtdIns3P levels and its PtdIns3P-specific PLA1 activity blocks endosomal and aut

34 d then phosphorylation by PtdIns3P 4-kinase (PtdIns3P 4-K), a novel pathway apparently contingent upo

35 s bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinosit

36 ions of the other negatively charged lipids, PtdIns3P, phosphatidic acid, and phosphatidyl-serine.

37 In yeast and mammals, PtdIns3P and PtdIns(3,5)P2 play crucial roles in traffic

38 s3,4,5P3 and reduced the cellular content of PtdIns3P by 50%.

39 Conversely, the disappearance of PtdIns3P that signals the transition from early to late

40 bind polyphosphoinositides) are a family of PtdIns3P- and PtdIns(3,5)P2-binding proteins that play a

41 dIns(3,4,5)P3, but to transient formation of PtdIns3P and generation of PtdIns(3,4)P2, the latter pri

42 through wortmannin-inhibitable generation of PtdIns3P and then phosphorylation by PtdIns3P 4-kinase (

43 pendent inhibition in the cellular levels of PtdIns3P and PtdIns3,4,5P3 with IC50 values of about 10

44 On local loss of PtdIns3P/PtdIns(3,5)P2, the endosomal compartment itself

45 By contrast, the maintenance of PtdIns3P levels, presumably involving a PtdIns-specific,

46 lpain inhibitors, and the phosphorylation of PtdIns3P by PtdIns3P 4-kinase.

47 t regulates production of a specific pool of PtdIns3P.

48 Atg6 in yeast, to regulate the production of PtdIns3P and autophagy.

49 these results, we propose that production of PtdIns3P by PI3K-C2alpha is required for acquisition of

50 kinase complexes, mediates the production of PtdIns3P, a key intracellular lipid involved in regulati

51 Selective reconstitution of PtdIns3P levels in cells lacking PI3K-C2alpha rescues Ra

52 nction of FYVE proteins as low pH sensors of PtdIns3P and reveals the critical role of the histidine

53 responsible for the stimulated synthesis of PtdIns3P observed in platelets.

54 partially dependent ( approximately 30%) on PtdIns3P binding to p40(phox), but totally dependent on

55 ding of EEA1 and decreases its dependence on PtdIns3P.

56 this response is substantially dependent on PtdIns3P-binding to p40(phox).

57 nse correlates with inhibition of phagosomal PtdIns3P accumulation and overlaps with the reduction in

58 e coincides with the emergence of phagosomal PtdIns3P.

59 RR-induced phosphatidylinositol 3-phosphate (PtdIns3P) and autophagy levels, thereby increasing PRR-i

60 ffinity to phosphatidylinositol-3-phosphate (PtdIns3P) and cleaves the fatty acid in PtdIns3P at the

61 sphorylate phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P(2), two phosphoinositides tha

62 sphorylate phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2, lipids which regulate endo-

63 nds to both phosphtidylinositol 3-phosphate (PtdIns3P) and to Rab5-GTP in vitro, but the functional r

64 duction of phosphatidylinositol 3-phosphate (PtdIns3P) by the lipid kinase VPS34/PIK3C3, the mechanis

65 contrast, phosphatidylinositol 3-phosphate (PtdIns3P) levels were unaffected.

66 it is the phosphatidylinositol 3-phosphate (PtdIns3P) or its metabolite PtdIns(3,5)P2 within this co

67 sumably for the product, PtdIns 3-phosphate (PtdIns3P), in the formation of secretory transport vesic

68 eration of phosphatidylinositol 3-phosphate (PtdIns3P), which is sensitive to wortmannin (IC50 7 nM)

69 gous to the phophatidylinositol 3-phosphate (PtdIns3P)-binding pocket of p40(phox), while the other b

70 gnition of phosphatidylinositol 3-phosphate [PtdIns3P] by the FYVE domain targets cytosolic proteins

71 tro dephosphorylates the 3-phosphoinositides PtdIns3P and PtdIns(3,5)P(2), with a preference for PtdI

72 eta-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5)P(2) using a conserved FRRG moti

73 sitol (PtdIns) 3-kinases (PI3Ks) can produce PtdIns3P to control endocytic trafficking, but whether e

74 orylate the D3 position of PtdIns to produce PtdIns3P.

75 I3K-C2alpha) and its main catalytic product, PtdIns3P, in regulated exocytosis.

76 alpha mutant or a 2xFYVE domain sequestering PtdIns3P abolished secretion.

77 We conclude that PtdIns3P-dependent lysosome translocation to the cell pe

78 The PtdIns3P 5-kinase Fab1 makes PtdIns(3,5)P(2), a phosphoi

79 tdIns(3,5)P(2) synthesis is catalyzed by the PtdIns3P 5-kinase Fab1p, and loss of this activity resul

80 s and endoplasmic reticulum that contain the PtdIns3P effector Protrudin.

81 e, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicati

82 d ArPIKfyve, the associated regulator of the PtdIns3P-5 kinase PIKfyve, form a stable binary complex

83 Amino acids stimulate recruitment of the PtdIns3P-binding protein FYCO1 to lysosomes and promote

84 gene, which selectively prevents binding to PtdIns3P.

85 PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosph

86 finger domain binds with high specificity to PtdIns3P and proteins containing this domain have been s

87 Whereas PtdIns3P binding only required the FYVE domain, Rab5 bin

88 stablished regulator of endocytosis, whereas PtdIns3P modulates endosomal trafficking.

89 C2-SAC5 localize to the tonoplast along with PtdIns3P, the presumable product of their activity.