FEATURES

FAMILY

DESCRIPTION

Also known as GID4_YEAST, VID24, GID4. Substrate-recognition component of the GID complex, a multisubunit ubiquitin ligase that targets enzymes involved in gluconeogenesis for proteasomal degradation when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:18508925, PubMed:28126757). Specific for substrates with an N-terminal Pro (Pro/N-degron), including FBP1, ICL1 and MDH2 (PubMed:28126757). Has high affinity for the N-terminal sequence Pro-Thr-Leu-Val, and can bind peptides with an N-terminal sequence of the type Pro-[Gly, Ala, Ser, Thr, Asp, Asn, Tyr, His]-[Ala, Val, Leu, Ile, Lys, Arg]-[Val, Cys, Pro, Leu, Ile, Trp] (PubMed:28126757). Required for vacuolar degradation of FBP1 when cells are shifted to glucose-containing medium, probably by targeting FBP1-containing vesicles to the vacuole, but is not required for FBP1 sequestration in cytoplasmic vesicles (PubMed:9508768). Substrate-recognition component of the GID ubiquitin ligase complex; interacts with proteins that have an N-terminal Pro/N-degron, including FBP1, ICL1 and MDH2 (PubMed:28126757). Identified in the GID complex, but only when cells are shifted to glucose-containing medium. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is recruited to the complex via interaction with VID28/GID5 (PubMed:22645139).

EXTERNAL LINKS

VID24

Vacuolar import and degradation protein 24

VID24

Molecular Synopsis