Golgi reassembly-stacking protein 2 (GORASP2)

Golgi reassembly-stacking protein 2 (GORASP2), also commonly known as GRASP55, is a peripheral membrane protein critical for the structural organization of the Golgi apparatus in human cells[1][3]. GORASP2 participates in the stacking of Golgi cisternae and the assembly of these stacks into a Golgi ribbon, a process essential for correct protein glycosylation and trafficking through the secretory pathway[1][3][7]. This protein forms homo-oligomers via its N-terminal GRASP domain, tethering adjacent cisternae together[1][3][7]. It is differentially regulated during the cell cycle; phosphorylation of its C-terminal SPR domain modulates Golgi disassembly during mitosis[1][3]. GORASP2 is also involved in trafficking specific membrane proteins, including transforming growth factor alpha, and plays a role in autophagy under glucose starvation, where it assists the fusion of autophagosomes and lysosomes[7]. Mutations or dysfunction in GORASP2 are linked to congenital disorders of glycosylation, male infertility, and alterations in glycoprotein processing[3][6]. GORASP2 is not currently considered a classical therapeutic target such as a receptor, enzyme, or transporter.

Other names

GRASP55GRS2GOLPH6p59Golgi phosphoprotein 6Golgi reassembly-stacking protein of 55 kDa