Golgi reassembly-stacking protein 1; Golgi peripheral membrane protein p65; Golgi phosphoprotein 5; GOLPH5; Golgi reassembly-stacking protein of 65 kDa; GRASP65 (GORASP1, GOLPH5, GRASP65)

Function: - stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments - key structural protein required for maintenance of Golgi integrity - its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis - mediates, via its interaction with GM130, docking of transport vesicles with Golgi membranes - phosphorylated by CDC2/cyclin B1 & PLK kinases during mitosis - phosphorylation cycle correlates with the cisternal stacking cycle - phosphorylation of the homodimer prevents association of dimers into higher order oligomers, leading to cisternal unstacking - target for caspase-3 cleavage during apoptosis - cleavage contributes to Golgi fragmentation & occurs very early in the execution phase of apoptosis (putative) - homodimer - forms higher order oligomers during interphase - does not form higher order oligomers during mitosis - dimers of the protein on one membrane might be able to interact with dimers on another & so stack cisternae - interacts with the C-terminus of GM130 (mitosis-independent) - role in targeting of both proteins to the cis-Golgi - the GORASP1/GM130 complex binds to vesicle docking protein p115 - interacts with TMED2 & TMED3 (putative) Structure: - belongs to the GORASP family - contains 1 PDZ domain (DHR domain) Compartment: - Golgi, cis-Golgi network membrane - peripheral membrane; cytoplasmic side - undergoes rapid exchange with the cytosol Alternative splicing: named isoforms=3

Properties

SIZE: entity length = 440 aa MW = 46 kD COMPARTMENT: cytoplasm golgi MOTIF: myristoylation site SITE: G2 EFFECTOR-BOUND: myristate PDZ domain NAME: PDZ domain SITE: 5-75 Essential for the interaction with GM130 {190-202} proline-rich region SITE: 203-298 MOTIF: proline residue (SEVERAL) Thr phosphorylation site {T216} Ser phosphorylation site {S243} Ser phosphorylation site {S248} proline-rich region SITE: 295-298 MOTIF: proline residue (SEVERAL) serine-rich region {348-352} MOTIF: serine residue (SEVERAL)

Database Correlations

OMIM 606867 UniProt Q9BQQ3 Pfam PF04495 Entrez Gene 64689 Kegg hsa:64689

References

UniProt :accession Q9BQQ3