|PROSITE documentation PDOC51865 [for PROSITE entry PS51865]|
The Golgi apparatus is a highly dynamic organelle responsible for sorting out proteins and other biomolecules to the cell surface and to the extracellular milieu. The Golgi apparatus is comprised of flattened membrane-bound compartments called cisternae, which are apposed to one another to form a Golgi stack. The structural organization of the cisternae into stacks and their lateral connection, building the Golgi ribbon, requires a family of proteins called Golgi ReAssembly and Stacking Proteins (GRASP). Two homologues (GRASP55 and GRASP65) have been described in vertebrates and their functions have been associated to Golgi phosphorylation-regulated assembly/disassembly, protein secretion , Golgi remodeling in migrating cells, among others. There is only one gene for GRASP in lower eukaryotes. Essentially all GRASPs contain a conserved N-terminal GRASP region, which comprises two tandem PDZ domains (PDZ1 and PDZ2), a classical protein-peptide interaction domain (see <PDOC50106>), and is responsible for GRASP homo-oligomerization and for the attachment to the Golgi membrane. The C-terminal half which is not conserved between species but is rich in proline and serines residues, as well as glutamine and asparagine residues [1,2,3,4].
The GRASP-type PDZ domains adopt a canonical PDZ fold with a β-sandwich of five β-strands and two α-helices (see <PDB:4KFW>). The PDZ1 and PDZ2 domains are nearly superimposable. The peptide-binding pockets of both PDZ domains are formed by α2 and β5. A typical ligand peptide is predicted to form antiparallel β-strand interactions with β5 and insert hydrophobic side chains between α2 and β5. The two PDZ domains cooperate to achieve dimerization and oligomerization. In the dimers the PDZ2 domains interact in a way that positions the peptide-binding pockets facing each other. In addition, the dimers are linked through interactions between the two C-terminal tails (CTs) of one dimer and two peptide-binding pockets of the PDZ1 domains in the next dimer [3,4].
The profile we developed covers the entire GRASP-type PDZ domain.Last update:
June 2018 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Mendes L.F.S. Garcia A.F. Kumagai P.S. de Morais F.R. Melo F.A. Kmetzsch L. Vainstein M.H. Rodrigues M.L. Costa-Filho A.J.|
|Title||New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.|
|Source||Sci. Rep. 6:29976-29976(2016).|
|2||Authors||Vinke F.P. Grieve A.G. Rabouille C.|
|Title||The multiple facets of the Golgi reassembly stacking proteins.|
|Source||Biochem. J. 433:423-433(2011).|
|3||Authors||Feng Y. Yu W. Li X. Lin S. Zhou Y. Hu J. Liu X.|
|Title||Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins.|
|Source||J. Biol. Chem. 288:28418-28427(2013).|
|4||Authors||Truschel S.T. Sengupta D. Foote A. Heroux A. Macbeth M.R. Linstedt A.D.|
|Title||Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis.|
|Source||J. Biol. Chem. 286:20125-20129(2011).|