Recombinant Human GORASP2 protein

GORASP2 (Golgi ReAssembly Stacking Protein 2), also known as GRASP55. is a ubiquitously expressed protein primarily localized to the Golgi apparatus. It plays a critical role in maintaining Golgi structure and regulating vesicular trafficking. As a member of the GRASP family, it contains N-terminal PDZ domains and a C-terminal SPCR motif, enabling its function in membrane tethering and stacking of Golgi cisternae. Unlike its paralog GRASP65 (GORASP1), which operates in the cis-Golgi, GRASP55 predominantly acts in the medial/trans-Golgi compartments.

Recombinant GORASP2 proteins are engineered to study Golgi dynamics, particularly in contexts like mitosis, cellular stress, or pathological conditions. Researchers produce these proteins using heterologous expression systems (e.g., E. coli, mammalian cells) with tags (e.g., His, GFP) for purification and tracking. Studies using recombinant GORASP2 have revealed its involvement in unconventional protein secretion, autophagy, and ER-Golgi communication. It also participates in O-glycosylation regulation and collagen export, linking it to developmental disorders and connective tissue diseases.

Notably, GORASP2 dysregulation is implicated in cancer progression and neurodegenerative diseases. Its phosphorylation status, modulated by kinases like CDK1 and PLK1 during cell cycle transitions, governs Golgi disassembly-reassembly cycles. Recombinant forms enable structural studies (e.g., crystallography) to map interaction interfaces and screen small-molecule modulators. Current research leverages GORASP2 recombinant proteins to dissect Golgi-related mechanisms in cellular homeostasis and develop therapeutic strategies targeting secretory pathway defects.