[HTML][HTML] Mapping the functional domains of the Golgi stacking factor GRASP65
The Golgi reassembly stacking protein (GRASP) family has been implicated in the stacking
of Golgi cisternae and the regulation of Golgi disassembly/reassembly during mitosis in
mammalian cells. GRASP65 is a dimer that can directly link adjacent surfaces through trans-
oligomerization in a mitotically regulated manner. Here we show that the N-terminal GRASP
domain (amino acids 1–201) is both necessary and sufficient for dimerization and trans-
oligomerization but is not mitotically regulated. The C-terminal serine/proline-rich domain …
of Golgi cisternae and the regulation of Golgi disassembly/reassembly during mitosis in
mammalian cells. GRASP65 is a dimer that can directly link adjacent surfaces through trans-
oligomerization in a mitotically regulated manner. Here we show that the N-terminal GRASP
domain (amino acids 1–201) is both necessary and sufficient for dimerization and trans-
oligomerization but is not mitotically regulated. The C-terminal serine/proline-rich domain …