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1 PtdIns3P 4-K is not the recently described "PIP5KIIalpha
2 PtdIns3P may play a role in modulating the Rab5 EEA1 int
5 s, PI3K-C2alpha regulates the formation of a PtdIns3P pool at the PRE required for Rab11 and Shh path
6 Substitution of the His residues abolishes PtdIns3P binding by the FYVE domain in vitro and in vivo
12 pellers that bind polyphosphoinositides) are PtdIns3P and PtdIns(3,5)P2 binding autophagy related pro
13 e suggested that all Fab1p homologues may be PtdIns3P 5-kinases involved in membrane trafficking.
14 N family members Atg18, Atg21, and Hsv2 bind PtdIns3P and PtdIns(3,5)P2 with high affinities in the n
18 y and activation is highly dependent on both PtdIns3P-p40(phox) and Rac2-p67(phox) interactions and d
19 tion of PtdIns3P and then phosphorylation by PtdIns3P 4-kinase (PtdIns3P 4-K), a novel pathway appare
27 sponse to platelet agonists, do not generate PtdIns3P or activate HsC2-PI3K under conditions that sti
28 ate (PtdIns3P) and cleaves the fatty acid in PtdIns3P at the sn1 position in vitro making it the firs
29 pression and, in turn, decreased PRR-induced PtdIns3P and autophagy and increased PRR-induced caspase
30 ression of ABH in vivo reduces intracellular PtdIns3P levels and its PtdIns3P-specific PLA1 activity
31 educes intracellular PtdIns3P levels and its PtdIns3P-specific PLA1 activity blocks endosomal and aut
32 d then phosphorylation by PtdIns3P 4-kinase (PtdIns3P 4-K), a novel pathway apparently contingent upo
33 ions of the other negatively charged lipids, PtdIns3P, phosphatidic acid, and phosphatidyl-serine.
37 bind polyphosphoinositides) are a family of PtdIns3P- and PtdIns(3,5)P2-binding proteins that play a
38 dIns(3,4,5)P3, but to transient formation of PtdIns3P and generation of PtdIns(3,4)P2, the latter pri
39 through wortmannin-inhibitable generation of PtdIns3P and then phosphorylation by PtdIns3P 4-kinase (
40 pendent inhibition in the cellular levels of PtdIns3P and PtdIns3,4,5P3 with IC50 values of about 10
46 these results, we propose that production of PtdIns3P by PI3K-C2alpha is required for acquisition of
47 kinase complexes, mediates the production of PtdIns3P, a key intracellular lipid involved in regulati
49 nction of FYVE proteins as low pH sensors of PtdIns3P and reveals the critical role of the histidine
51 partially dependent ( approximately 30%) on PtdIns3P binding to p40(phox), but totally dependent on
54 nse correlates with inhibition of phagosomal PtdIns3P accumulation and overlaps with the reduction in
56 RR-induced phosphatidylinositol 3-phosphate (PtdIns3P) and autophagy levels, thereby increasing PRR-i
57 ffinity to phosphatidylinositol-3-phosphate (PtdIns3P) and cleaves the fatty acid in PtdIns3P at the
58 sphorylate phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P(2), two phosphoinositides tha
59 sphorylate phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2, lipids which regulate endo-
60 nds to both phosphtidylinositol 3-phosphate (PtdIns3P) and to Rab5-GTP in vitro, but the functional r
61 duction of phosphatidylinositol 3-phosphate (PtdIns3P) by the lipid kinase VPS34/PIK3C3, the mechanis
63 it is the phosphatidylinositol 3-phosphate (PtdIns3P) or its metabolite PtdIns(3,5)P2 within this co
64 sumably for the product, PtdIns 3-phosphate (PtdIns3P), in the formation of secretory transport vesic
65 eration of phosphatidylinositol 3-phosphate (PtdIns3P), which is sensitive to wortmannin (IC50 7 nM)
66 gous to the phophatidylinositol 3-phosphate (PtdIns3P)-binding pocket of p40(phox), while the other b
67 gnition of phosphatidylinositol 3-phosphate [PtdIns3P] by the FYVE domain targets cytosolic proteins
68 eta-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5)P(2) using a conserved FRRG moti
69 sitol (PtdIns) 3-kinases (PI3Ks) can produce PtdIns3P to control endocytic trafficking, but whether e
75 tdIns(3,5)P(2) synthesis is catalyzed by the PtdIns3P 5-kinase Fab1p, and loss of this activity resul
77 e, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicati
78 d ArPIKfyve, the associated regulator of the PtdIns3P-5 kinase PIKfyve, form a stable binary complex
81 finger domain binds with high specificity to PtdIns3P and proteins containing this domain have been s
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