Glucose-induced degradation protein 8 homolog (GID8)

Glucose-induced degradation protein 8 homolog (GID8) is a core component of the CTLH (C-terminal to LisH) E3 ubiquitin-protein ligase complex, which is responsible for substrate recognition, ubiquitin transfer, and mediating proteasomal degradation of specific transcription factors—most notably HBP1. GID8 plays a crucial role in **regulating the canonical Wnt signaling pathway** by acting as a nuclear retention factor for β-catenin. Upon Wnt stimulation, GID8/Twa1 facilitates the nuclear accumulation and retention of β-catenin, which is essential for Wnt-regulated transcriptional activation involved in cell proliferation and tumorigenesis. Upregulation of nuclear GID8 is correlated with increased β-catenin nuclear localization and poor prognosis in colorectal cancer. It participates in protein homodimerization and positively regulates cell population proliferation. GID8 is not a classic receptor or enzyme but functions in multiprotein complexes associated with cell signaling and protein degradation. There are no known drugs that selectively target GID8, and it is not established as a drug target or clinical biomarker.

Other names

C20orf11TWA1Two hybrid-associated protein 1 with RanBPMFLJ20602bA305P22.1Two hybrid associated protein No. 1 with RanBPMprotein C20orf11GID complex subunit 8 homologTwa1