PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24165940-2 2013 Autophagy is characterized by the formation of an autophagosome, for which Vps34-dervied phosphatidylinositol 3-phosphate (PI3P) is essential. phosphatidylinositol 3-phosphate 89-121 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 75-80 10021387-4 1999 Another of these proteins, Vac1p/Pep7p/Vps19p, associates with Pep12p and binds phosphatidylinositol 3-phosphate (PI(3)P), the product of the Vps34 phosphatidylinositol 3-kinase (PI 3-kinase) [1] [2]. phosphatidylinositol 3-phosphate 80-112 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 142-147 18769150-6 2008 Endosomal recruitment of all three proteins depends on PtdIns3P generated by the Vps34-complex II containing Vps38p, but not on the function of the Vps34-complex I. phosphatidylinositol 3-phosphate 55-63 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 81-86 18533003-2 2008 Here, we show that the lipid-kinase activity of Vps34 is required for autophagy, implying an essential role of its product PtdIns(3)P. phosphatidylinositol 3-phosphate 123-133 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 48-53 12244127-1 2002 A direct role for phosphoinositides in vesicular trafficking has been demonstrated by the identification of the yeast VPS34 gene encoding the phosphatidylinositol 3-kinase responsible for the synthesis of phosphatidylinositol 3-phosphate (PtdIns3P). phosphatidylinositol 3-phosphate 205-237 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 118-123 12244127-1 2002 A direct role for phosphoinositides in vesicular trafficking has been demonstrated by the identification of the yeast VPS34 gene encoding the phosphatidylinositol 3-kinase responsible for the synthesis of phosphatidylinositol 3-phosphate (PtdIns3P). phosphatidylinositol 3-phosphate 239-247 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 118-123 23335340-2 2013 We found that yeast mutants lacking the phosphatidylinositol 3-phosphate [PI(3)P] kinase Vps34 or its associated protein kinase Vps15 display multiple phenotypes indicating impaired transcription elongation. phosphatidylinositol 3-phosphate 40-72 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 89-94 22121197-8 2012 The lack of Vps34p resulted in the absence of phosphatidylinositol 3-phosphate, a lipid required for SNARE activity and vacuole fusion. phosphatidylinositol 3-phosphate 46-78 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 12-18 21121900-2 2011 We have discovered a PtdIns3P-synthesizing activity in peroxisomes of Saccharomyces cerevisiae and have demonstrated that the lipid kinase Vps34p is already associated with peroxisomes during biogenesis. phosphatidylinositol 3-phosphate 21-29 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 139-145 10021387-4 1999 Another of these proteins, Vac1p/Pep7p/Vps19p, associates with Pep12p and binds phosphatidylinositol 3-phosphate (PI(3)P), the product of the Vps34 phosphatidylinositol 3-kinase (PI 3-kinase) [1] [2]. phosphatidylinositol 3-phosphate 114-120 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 142-147 33309995-8 2021 This is supported by our observation that the presence of excess leucine, a known activator of the lipid kinase responsible for the generation of PI3-P, Vps34, in the medium can rescue the CSE-induced ESCRT misfunctioning. phosphatidylinositol 3-phosphate 146-151 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 153-158 34798133-1 2022 Phosphatidylinositol 3-phosphate (PI3P), a scaffold of membrane-associated proteins required for diverse cellular events, is produced by Vps34-containing phosphatidylinositol 3-kinase (PI3K). phosphatidylinositol 3-phosphate 0-32 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 137-142 34798133-1 2022 Phosphatidylinositol 3-phosphate (PI3P), a scaffold of membrane-associated proteins required for diverse cellular events, is produced by Vps34-containing phosphatidylinositol 3-kinase (PI3K). phosphatidylinositol 3-phosphate 34-38 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 137-142 9838078-6 1998 PtdIns 3-P is produced by Vps34p/class III PI3Ks and operates via the PtdIns 3-P-binding proteins early endosomal antigen (EEA1), yeast Vac1p, Vps27p, Pip1p in lysosomal protein targeting. phosphatidylinositol 3-phosphate 0-10 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 26-32 9763421-6 1998 The presence of PtdIns(3)P in fab1 mutants, combined with previous data, indicate that PtdIns(3,5)P2 synthesis is a two step process, requiring the production of PtdIns(3)P by the Vps34p PtdIns 3-kinase and the subsequent Fab1p- dependent phosphorylation of PtdIns(3)P yielding PtdIns(3,5)P2. phosphatidylinositol 3-phosphate 162-172 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 180-186 9763421-6 1998 The presence of PtdIns(3)P in fab1 mutants, combined with previous data, indicate that PtdIns(3,5)P2 synthesis is a two step process, requiring the production of PtdIns(3)P by the Vps34p PtdIns 3-kinase and the subsequent Fab1p- dependent phosphorylation of PtdIns(3)P yielding PtdIns(3,5)P2. phosphatidylinositol 3-phosphate 162-172 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 180-186 9763421-7 1998 Although Vps34p-mediated synthesis of PtdIns(3)P is required for the proper sorting of hydrolases from the Golgi to the vacuole, the production of PtdIns(3,5)P2 by Fab1p does not directly affect Golgi to vacuole trafficking, suggesting that PtdIns(3,5)P2 has a distinct function. phosphatidylinositol 3-phosphate 38-48 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 9-15 7721937-8 1995 This rapid block in vacuolar protein sorting appears to be the result of loss of PtdIns 3-kinase activity since cellular PtdIns(3)P levels decrease dramatically in vps34 temperature-sensitive mutant cells that have been incubated at the nonpermissive temperature. phosphatidylinositol 3-phosphate 121-131 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 164-169 34831348-3 2021 PtdIns(3)P is synthesized from phosphatidylinositol (PtdIns) by PIK3C3C/VPS34 in mammals or Vps34 in yeast. phosphatidylinositol 3-phosphate 0-10 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 72-77 34831348-3 2021 PtdIns(3)P is synthesized from phosphatidylinositol (PtdIns) by PIK3C3C/VPS34 in mammals or Vps34 in yeast. phosphatidylinositol 3-phosphate 0-10 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 92-97 33459128-4 2021 In order to synthesize PtdIns3P for the initiation of autophagy, PIK3C3/Vps34 has a heterotetrameric core, the PIK3C3 complex I (hereafter complex I) composed of PIK3C3/Vps34, PIK3R4/Vps15, BECN1/Vps30, and ATG14/Atg14. phosphatidylinositol 3-phosphate 23-31 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 72-77 33459128-4 2021 In order to synthesize PtdIns3P for the initiation of autophagy, PIK3C3/Vps34 has a heterotetrameric core, the PIK3C3 complex I (hereafter complex I) composed of PIK3C3/Vps34, PIK3R4/Vps15, BECN1/Vps30, and ATG14/Atg14. phosphatidylinositol 3-phosphate 23-31 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 169-174 33237833-5 2021 To test this hypothesis, we elevated the levels of phosphatidylinositol-3-phosphate (PI3P) by generating hyperactive alleles of the yeast phosphatidylinositol 3-kinase, Vps34. phosphatidylinositol 3-phosphate 51-83 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 169-174 33237833-5 2021 To test this hypothesis, we elevated the levels of phosphatidylinositol-3-phosphate (PI3P) by generating hyperactive alleles of the yeast phosphatidylinositol 3-kinase, Vps34. phosphatidylinositol 3-phosphate 85-89 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 169-174 28483912-8 2017 Using this system, we found that this mechanism specifically responds to l-glutamine, resides on the vacuolar membranes, and involves a previously uncharacterized Vps34-Vps15 phosphatidylinositol (PI) 3-kinase complex and the PI-3-phosphate [PI(3)P]-binding FYVE domain-containing vacuolar protein Pib2. phosphatidylinositol 3-phosphate 226-240 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 163-168 29967628-2 2018 In animals and yeast, PtdIn-3-phosphate, which is particularly important for endosomal sorting, lysosomal/vacuolar transport and autophagy, is assembled by two conserved kinase complexes comprised of the catalytic VACUOLAR PROTEIN SORTING (VPS)-34 subunit, along with VPS15, AUTOPHAGY-RELATED (ATG)-6, and either ATG14 (complex I) or VPS38 (complex II). phosphatidylinositol 3-phosphate 22-39 phosphatidylinositol 3-kinase VPS34 Saccharomyces cerevisiae S288C 214-247