Protein Variants | Comment | Organism |
---|---|---|
additional information | ppk-3(n2668) strong loss-of-function mutants embryos contain many vacuolar structures of different sizes, a subset of which are positive for both LAAT-1::GFP and HIS-24::mCh, indicating that they are phagolysosomes. The double mutant of slc-36.1(yq110) with ppk-3(n2668) contains enlarged autolysosomes similar to ppk-3(n2668) single mutants | Caenorhabditis elegans |
S1448L | naturally occuring mutation yq24, yq24 mutants exhibit embryonic vacuoles similar to slc-36.1 mutants. Double mutants of yq24 with ced-4(n1162) show neither button-like apoptotic cell corpses nor vacuolar structures. The yq24 embryonic vacuoles are enriched for both LAAT-1::GFP and HIS-24::mCh. Mutant yq24 embryonic vacuoles are phagolysosomes arising from apoptosis | Caenorhabditis elegans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Caenorhabditis elegans | 5764 | - |
vacuole | lysosomal | Caenorhabditis elegans | 5773 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Caenorhabditis elegans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | Caenorhabditis elegans | - |
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Caenorhabditis elegans | G5ED98 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | - |
Caenorhabditis elegans | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate | - |
Caenorhabditis elegans | ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PIKfyve | - |
Caenorhabditis elegans |
PPK-3 | - |
Caenorhabditis elegans |
PtdIns3P 5-kinase | - |
Caenorhabditis elegans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Caenorhabditis elegans |
General Information | Comment | Organism |
---|---|---|
malfunction | loss of PPK-3, the Caenorhabditis elegans homologue of the PtdIns3P 5-kinase PIKfyve, causes accumulation of phagolysosomal vacuoles that are defective in phagocytic lysosome reformation (PLR). Loss of slc-36.1 and ppk-3 causes strong defects in autophagic lysosome reformation in adult animals. Ppk-3(n2668) strong loss-of-function mutants embryos contain many vacuolar structures of different sizes, a subset of which are positive for both LAAT-1::GFP and HIS-24::mCh, indicating that they are phagolysosomes. The double mutants of slc-36.1(yq110) with ppk-3(n2668) contain enlarged autolysosomes similar to ppk-3(n2668) single mutants | Caenorhabditis elegans |
metabolism | amino acid transporter SLC-36.1 and PPK-3 function in the same genetic pathway, and they directly interact with one another. The SLC-36.1-PPK-3 axis is essential for autophagic lysosome reformation (ALR) | Caenorhabditis elegans |
physiological function | the phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase PIKfyve and the lysosomal calcium channel TRPML1 are required for endocytic lysosome reformation. PIKfyve generates phosphatidylinositol 3,5-bisphosphate, which activates TRPML1 to control lysosomal Ca2+ efflux. The SLC-36.1-PPK-3 axis is essential for ALR | Caenorhabditis elegans |