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The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum.
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GRASP65 phosphorylation may have a critical role in inducing cell death.
In situ proximity ligation assays of Golgi localization of alpha-mannosidase IA at giantin (zeige GOLGB1 Antikörper) versus GM130 (zeige GOLGA2 Antikörper)-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.
Results demonstrate a critical role for GRASP55 (zeige GORASP2 Antikörper) 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.
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 (zeige CISH Antikörper)-Golgi protein (zeige GOLPH3 Antikörper), Grasp65.
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.
Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 (zeige GOLGA2 Antikörper) association.
Cisternal-specific functions of GRASP65 and GRASP55 (zeige GORASP2 Antikörper) in continuity, compartmentalization, and function of the Golgi ribbon.
propose that GRASP55 (zeige GORASP2 Antikörper)/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
The C-terminal fragments of GRASP65 produced following caspase (zeige CASP3 Antikörper) cleavage are targeted to mitochondria, and ectopic expression of these sensitises HeLa cells to Fas ligand (zeige FASL Antikörper).
the mechanism of phosphoinhibition as direct inhibition by PLK1 (zeige PLK1 Antikörper) of the PDZ (zeige INADL Antikörper) ligand underlying the GRASP65 self-interaction.
GRASP65 has a role in Golgi cisternal stacking and cell cycle progression
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a membrane protein involved in establishing the stacked structure of the Golgi apparatus. It is a caspase-3 substrate, and cleavage of this encoded protein contributes to Golgi fragmentation in apoptosis. This encoded protein can form a complex with the Golgi matrix protein GOLGA2, and this complex binds to the vesicle docking protein p115. Several alternatively spliced transcript variants of this gene have been identified, but their full-length natures have not been determined.
Golgi reassembly-stacking protein 1
, golgi reassembly stacking protein 1, 65kDa
, golgi reassembly stacking protein 1
, golgi reassembly-stacking protein 1-like
, Golgi reassembly-stacking protein 1-like
, golgi perepheral membrane protein p65
, golgi peripheral membrane protein p65
, golgi reassembly-stacking protein of 65 kDa
, Golgi peripheral membrane protein p65
, Golgi phosphoprotein 5
, Golgi reassembly and stacking protein 1