Transport of glycosylphosphatidylinositol-anchored proteins from the endoplasmic reticulum

In this review on the transport of glycosylphosphatidylinositol-anchored proteins (GPI-APs), we focus on events that occur in the endoplasmic reticulum after the transfer of GPI to proteins. These events include structural remodeling of both the lipid and glycan moieties of GPI, recruitment of GPI-APs into ER exit sites, association with the cargo receptor, p24 protein complex, and packaging into COPII coated transport vesicles. Similarities with the transport of Wnt proteins are also discussed. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

► After attachment to proteins both lipid and glycan of GPI anchors are remodeled. ► Remodeling of GPI is required for efficient sorting into ERES and COPII coated vesicles. ► A complex of p24 family proteins acts as a cargo receptor for GPI-AP. ► GPI-AP and Wnt proteins are lipid-modified and transported similarly from the ER.