WebThe Golgi stacking proteins, GRASP55 and GRASP65, are best known for their roles in Golgi structure formation. These peripheral Golgi proteins form trans -oligomers that hold the flat cisternal membranes into stacks. WebAug 16, 2024 · Golgi reassembly stacking protein of 65 kDa (GRASP65) and Golgi reassembly stacking protein of 55 kDa (GRASP55) were originally identified as Golgi stacking proteins; however, subsequent GRASP knockdown experiments yielded inconsistent results with respect to the Golgi structure, indicating a limitation of RNAi …
Structural Basis for the Interaction between the Golgi …
WebFor example, GRASP65 (Golgi reassembly and stacking proteins 65), distributed on the peripheral membrane of the Golgi apparatus, interacts with the actin-binding protein Mena and leads to its own homologous oligomerization, which mediates the stacking of the Golgi cisternae and ribbon formation [122,123,124]. WebSep 9, 2024 · For example, Golgi coiled-coil protein (GCC)88 and Golgin subfamily A member 2 (GM130) play negative regulatory roles in formation and degradation of autophagosomes, while p230, WW domain … richardsons facebook
GRASP55 and GRASP65 play complementary and essential roles in Golgi ...
WebA novel mechanism for Golgi stacking is proposed.Significance: A novel interaction mode permits us to propose a new molecular basis for Golgi structure. Structural Basis for the … WebJun 22, 2024 · The data showed that the Golgins appeared in evolution and were anchored by the single GRASP ancestor before gorasp gene duplication and divergence in Metazoans, and it is suggested that the capacity of GRASPs to form supramolecular structures is a long-standing feature, which likely affectsGRASP’s participation as a … WebFeb 17, 2024 · open access. Golgin45 is required for normal Golgi structure and the transportation of protein from the ER. It forms a specific complex with GRASP55 in vivo. … redmond hud