Gyp7 is a GAP that catalyzes the hydrolysis of GTP to GDP on Ypt7, a Rab7 homolog in yeast. This activity is critical for regulating endosomal membrane dynamics and vacuole morphology . Gyp7 exhibits substrate specificity for Ypt7, despite earlier reports of low in vitro substrate specificity .
Endosomal Regulation: Gyp7 localizes to punctate endosomal structures near the vacuole, where it modulates Ypt7 activity .
TORC1 Signaling: Overexpression of Gyp7 retains Ypt7 on late endosomes, enhancing endosomal TORC1 signaling and conferring resistance to rapamycin .
Vacuole Morphology: Mistargeting Gyp7 to the vacuole disrupts vacuolar structure, indicating its essential role in endosomal function .
Gyp7 exhibits strong membrane affinity, which enhances its GAP activity toward membrane-bound Ypt7 .
Endosomal Puncta: Gyp7 concentrates in Class E compartments, colocalizing with endosomal markers (Vps21, Vps35) but not vacuolar markers .
Lipid Environment: Gyp7 requires specific lipid compositions for membrane binding and activity, as demonstrated by in vitro assays .
Gyp7 contains a Tre/Bub2/Cdc16 (TBC) domain with a catalytic arginine-glutamine finger, enabling GTP hydrolysis on Ypt7 .
Ypt7 Retention: Overexpression traps Ypt7 on late endosomes, disrupting normal endolysosomal transport .
TORC1 Activation: These Ypt7-positive endosomes lack ESCRT components but require ESCRTs for their formation .
KEGG: spo:SPAC630.05
STRING: 4896.SPAC630.05.1