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In situ proximity ligation assays of Golgi localization of alpha-mannosidase IA at giantin versus GM130-GRASP65 site, and absence or presence of N-glycans terminated with alpha3-mannose on trans-Golgi glycosyltransferases may be useful for distinguishing indolent from aggressive prostate cancer cells.
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Results demonstrate a critical role for GRASP55 and GRASP65 in maintaining the stacked structure of the Golgi, which is required for accurate posttranslational modifications in the Golgi. Additionally, the GRASP knockout cell lines developed in this study will be useful tools for studying the role of GRASP proteins in other important cellular processes.
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The authors determined that Golgi membrane ribbon fragmentation increased during the early cytoplasmic phase of cytomegalovirus virion assembly and that Golgi membrane fragmentation in infected cells was dependent on the phosphorylation of an integral cis-Golgi protein, Grasp65.
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In cells, Mena and actin were required for Golgi ribbon formation after nocodazole washout; in vitro, Mena and microfilaments enhanced GRASP65 oligomerization and Golgi membrane fusion. Thus Mena interacts with GRASP65 to promote local actin polymerization, which facilitates Golgi ribbon linking.
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Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.
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Cisternal-specific functions of GRASP65 and GRASP55 in continuity, compartmentalization, and function of the Golgi ribbon.
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propose that GRASP55/65 are negative regulators of exocytic transport and that this slowdown helps to ensure more complete protein glycosylation in the Golgi stack and proper sorting at the trans-Golgi network
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The C-terminal fragments of GRASP65 produced following caspase cleavage are targeted to mitochondria, and ectopic expression of these sensitises HeLa cells to Fas ligand.
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the mechanism of phosphoinhibition as direct inhibition by PLK1 of the PDZ ligand underlying the GRASP65 self-interaction.
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GRASP65 has a role in Golgi cisternal stacking and cell cycle progression
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These results demonstrate that GRASP55 and GRASP65 stack mammalian Golgi cisternae via a common mechanism.
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Data demonstrate that both GRASP55 and 65 are needed for the efficient transport to and through the Golgi complex, thus highlighting a novel role for the GRASPs in membrane trafficking.
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the GRASP domain alone of GRASP65 inhibits mitotic fragmentation of the Golgi apparatus
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GRASP65 may function as a signal integrator controlling the cell growth
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GRASP65 has a role in the regulation of spindle dynamics rather than a direct role in the stacking of Golgi cisternae
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Ribbon formation requires the Golgi proteins GM130 and GRASP65.
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Mitochondria bearing GRASP65 became tethered to one another, and this depended on a GRASP65 PDZ domain that was also required for GRASP65 self-interaction.
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A study showing that GRASP65 binds directly to the coiled-coil vesicle tethering factor GM130, and targets it to Golgi membranes.
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Identification of GRASP65, and demonstration that it functions in the formation of stacked Golgi cisternae.
