Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]

Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]

Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Autophagy-related protein 18; Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P- granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bis [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Protein lgg-1; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy. Recruits lipidated-lgg-2 to maturing autophagosomes. Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular, binds to components of the unc-51- [...]

Ubiquitin-like protein atg-12; Ubiquitin-like protein involved in autophagy vesicles formation (By similarity). Conjugation with atg-5 through a ubiquitin- like conjugating system involving also atg-7 as an E1-like activating enzyme and atg-10 as an E2-like conjugating enzyme, is essential for its function (By similarity). Most likely a component of an atg-5-lgg- 3-atg-16 complex that promotes autophagosome formation by associating with lgg-2, but not lgg-1, at the preautophagosomal membrane. Probably, as part of an atg-5-lgg- 3-atg-16 complex, required for lgg-1 lipidation; the comple [...]

Protein lgg-2; Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion. Less effective at promoting membrane fusion than lgg-1. Acts upstream of the autophagy protein epg-5 in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation. In particular binds to [...]