GORASP1
GORASP1 (golgi reassembly stacking protein 1, also known as GRASP65, P65 and GOLPH5) is a membrane protein of the Golgi apparatus that helps cisternae adhere into stacks and supports formation of the Golgi ribbon. Browse Assay Genie's current range of GORASP1 research reagents below, or read on for the biology behind the target.
GORASP1 is a key structural protein of the Golgi apparatus. Golgi membrane cisternae adhere to one another to form stacks, and these stacks are aligned side by side to form the Golgi ribbon. Acting together with GORASP2 (GRASP55), GORASP1 is required for formation and maintenance of the ribbon, and may be dispensable for stack formation itself. Other studies suggest it plays an important part in cisternal assembly and membrane stacking, and in reassembly of Golgi stacks after their breakdown in mitosis.
The protein also takes part in vesicle traffic. Through its interaction with GOLGA2 (GM130), GORASP1 mediates docking of transport vesicles with Golgi membranes. NCBI describes a complex of GORASP1 and GOLGA2 that binds the vesicle docking protein p115. In addition, GORASP1 mediates ER stress-induced unconventional, ER/Golgi-independent trafficking of core-glycosylated CFTR to the cell membrane. The protein localises to the cis-Golgi network membrane and the endoplasmic reticulum-Golgi intermediate compartment membrane.
The human GORASP1 gene encodes a member of the GORASP family, classed by HGNC in the PDZ domain containing group; alternative splicing gives multiple transcript variants. GORASP1 is a caspase-3 substrate, and caspase-mediated cleavage is required for Golgi fragmentation during apoptosis. Earlier names include golgi phosphoprotein 5 and golgi reassembly stacking protein 1, 65kDa, which explain the aliases GOLPH5 and GRASP65. Mouse and rat both carry a Gorasp1 ortholog.
GORASP1 helps cisternae stack and supports the Golgi ribbon, making it a focus for studies of Golgi structure.
Studies suggest GORASP1 contributes to reassembly of Golgi stacks after breakdown during mitosis.
Caspase-mediated cleavage of GORASP1 is required for Golgi fragmentation during apoptosis.
GORASP1 interacts with GOLGA2 to dock transport vesicles and mediates ER stress-induced unconventional CFTR trafficking.
GORASP1 is a structural protein of the Golgi apparatus. It helps membrane cisternae adhere into stacks and, with GORASP2, supports formation and maintenance of the Golgi ribbon. Via GOLGA2 it also mediates docking of transport vesicles with Golgi membranes.
GORASP1 is also called GRASP65, P65, FLJ23443 and GOLPH5. Previous names include golgi phosphoprotein 5 and golgi reassembly stacking protein 1, 65kDa. The UniProt entry is Golgi reassembly-stacking protein 1, and NCBI notes that alternative splicing yields multiple transcript variants.
Mouse and rat each have a Gorasp1 ortholog; check the datasheet of any product for its validated reactivity. GORASP1 is a caspase-3 substrate, and its caspase-mediated cleavage is required for Golgi fragmentation during apoptosis.
Golgi stacking partners, vesicle docking factors and apoptosis-pathway proteins linked to GORASP1 biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9BQQ3; product specifications from Assay Genie datasheets.