| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.71979534 |
| Vesicle mediated protein transport : regulatory interactions between the Vps 15 protein kinase and the Vps 34 PtdIns 3 kinase essential for protein sorting to the vacuole in yeast . 0.71979534^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| The Vps 15 protein kinase and the Vps 34 phosphatidylinositol 3 kinase have been shown to function as a membrane associated complex which facilitates the delivery of proteins to the vacuole in yeast . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| A membrane associated complex containing the Vps 15 protein kinase and the Vps 34 PI 3 kinase is essential for protein sorting to the yeast lysosome like vacuole . ^^^ The Vps 15 protein kinase and the Vps 34 phosphatidylinositol 3 kinase ( PI 3 kinase ) are required for the sorting of soluble hydrolases to the yeast vacuole . ^^^ In addition , we show that an intact Vps 15 protein kinase domain is required for activation of the Vps 34 PI 3 kinase , suggesting that the Vps 34 lipid kinase is regulated by a Vps15p mediated protein phosphorylation event . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| The VPS 15 and VPS 34 genes encode components of a novel signal transduction complex essential for the delivery of soluble vacuolar hydrolases . ^^^ VPS 15 and VPS 34 encode a serine / threonine protein kinase and a phosphatidylinositol 3 kinase , respectively , that interact at the cytoplasmic face of an intracellular membrane compartment , most likely corresponding to the late Golgi . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| Biochemical fractionation experiments have established that Ycf1p , expressed at single copy gene levels , co fractionates with the vacuolar membrane and that this co fractionation is independent of vps 15 , vps 34 or end 3 gene function . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| While yeast cells deficient in PI3K activity ( vps 15 and vps 34 mutants ) were not labelled , PI ( 3 ) P was found on intralumenal vesicles of endosomes and vacuoles of wild type yeast . vps27Delta yeast cells , which have impaired endosome to vacuole trafficking , showed a decreased vacuolar labelling and increased endosome labelling . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| The vps 34 and vps 15 mutants displayed additional phenotypes such as defects in transport of proteinase A and proteinase B , implying the existence of another PtdIns 3 kinase complex ( es ) . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| First , we show that transient disruption of phosphatidylinositol ( PtdIns ) 3 phosphate ( PtdIns [ 3 ] P ) synthesis through inactivation of temperature sensitive Vps 34 or its upstream activator , Vps 15 , blocks the Cvt and macroautophagy pathways . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| Recent data on two of these genes , VPS 15 and VPS 34 , are beginning to provide some fundamental insights into the mechanisms governing protein sorting within the eukaryotic secretory pathway . ^^^ VPS 15 and VPS 34 encode a novel protein kinase and a phosphatidylinositol 3 kinase , respectively , that function together as components of a membrane associated signal transduction complex . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| Using genetic analysis , we characterized the pathway by which VPS 15 , VPS 34 , VPS 22 , VPS 23 and VPS 28 affect the telomeres . ^^^ |
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| Interacting proteins: Q8NEB9 and Q99570 |
Pubmed |
SVM Score :0.0 |
| Our analysis reveals a requirement for both the catalytic ( Vps 34 ) and regulatory ( Vps 15 ) subunits of the sole phosphatidylinositol 3 kinase in yeast . ^^^ We demonstrate that Gpa 1 is present at endosomes , where it interacts directly with both Vps 34 and Vps 15 and stimulates increased production of phosphatidylinositol 3 phosphate . ^^^ |
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