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Golgi reassembly-stacking protein 1 (GORASP1), also known as GRASP65, is a peripheral membrane protein essential for maintaining the structure and organization of the Golgi apparatus in vertebrate cells[1][2][3][4][5]. It contributes to the stacking and lateral linking of Golgi cisternae, forming the Golgi ribbon[1][3][4]. GORASP1 is myristoylated at its N-terminus, contains two PDZ domains, and interacts with proteins such as GM130, GOLGA2, and p115 to facilitate Golgi membrane fusion, vesicle tethering, and protein trafficking[1][2][3][4]. During apoptosis, it is cleaved by caspase-3, promoting Golgi fragmentation[1][3]. GORASP1, together with its paralog GORASP2 (GRASP55), has been implicated in unconventional secretion pathways and cell cycle regulation[3][4]. Mutations or dysfunction of GORASP1 are associated with certain developmental disorders including Smith-McCort dysplasia and achondrogenesis[3].
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