Golgi reassembly-stacking protein of 65 kDa (GRASP65) also known as Golgi reassembly-stacking protein 1 (GORASP1) is a protein that in humans is encoded by the GORASP1gene.[1]
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The GRASP65 protein is a peripheral membrane protein anchored to the lipid bilayer through myristoylation of a glycine residue near the protein's amino terminus.[3] It is involved in establishing the stacked structure of the Golgi apparatus and linking the stacks into larger ribbons in verterbate cells.[3] It is a caspase-3 substrate, and cleavage of this encoded protein contributes to Golgi fragmentation in apoptosis.[4][5] GRASP65 can form a complex with the Golgi matrix protein GM130, and this complex binds to the vesicle docking protein p115.[3][lower-alpha 1] Several alternatively spliced transcript variants of this gene have been identified, but their full-length natures have not been determined.[1]
Barr FA, Puype M, Vandekerckhove J, Warren G (October 1997). "GRASP65, a protein involved in the stacking of Golgi cisternae". Cell. 91 (2): 253–62. doi:10.1016/S0092-8674(00)80407-9. PMID9346242.
Jesch SA (July 2002). "Inheriting a structural scaffold for Golgi biosynthesis". BioEssays. 24 (7): 584–7. doi:10.1002/bies.10122. PMID12111718.
Protopopov A, Kashuba V, Zabarovska VI, Muravenko OV, Lerman MI, Klein G, Zabarovsky ER (January 2003). "An integrated physical and gene map of the 3.5-Mb chromosome 3p21.3 (AP20) region implicated in major human epithelial malignancies". Cancer Research. 63 (2): 404–12. PMID12543795.
Wang Y, Satoh A, Warren G (February 2005). "Mapping the functional domains of the Golgi stacking factor GRASP65". The Journal of Biological Chemistry. 280 (6): 4921–8. doi:10.1074/jbc.M412407200. PMID15576368.
Yoshimura S, Yoshioka K, Barr FA, Lowe M, Nakayama K, Ohkuma S, Nakamura N (June 2005). "Convergence of cell cycle regulation and growth factor signals on GRASP65". The Journal of Biological Chemistry. 280 (24): 23048–56. doi:10.1074/jbc.M502442200. PMID15834132.