Trafficking protein particle complex subunit 8 (TRAPPC8)

Trafficking protein particle complex subunit 8 (TRAPPC8) is a large, TRAPPIII-specific subunit that serves a critical scaffolding and regulatory role within the TRAPPIII tethering complex, which mediates intracellular membrane trafficking. The protein is evolutionarily conserved and directly involved in endoplasmic reticulum (ER)-to-Golgi transport, organization of the Golgi apparatus, modulation of autophagy, and maintenance of ER homeostasis, particularly under stress conditions[1][2]. TRAPPC8 contains a Rab1-binding site important for the guanine nucleotide exchange factor (GEF) activity of TRAPPIII and a membrane-binding domain, essential for its cellular localization and function[1]. It has functional roles in selective autophagy and cytoplasm-to-vacuole targeting and is implicated in the formation and regulation of centriolar satellites and ciliogenesis, with its depletion causing abnormal ciliary assembly and morphology[2]. While mutations in TRAPPC8 result in notable developmental and trafficking defects in plant and animal models, there is no direct evidence linking it to specific human diseases as a primary causative gene or as a druggable target[1][2].

Other names

TRAPPC8KIAA1012TRS85GSG1HsT2706Protein TRS85 homologGeneral sporulation gene 1 homolog (from S. cerevisiae)