The Golgi apparatus: 100 years of progress and controversy

Farquhar, Marilyn G.; Palade, George E.

doi:10.1016/s0962-8924(97)01187-2

Cited by 284 publications

(181 citation statements)

References 88 publications

Supporting

Mentioning

172

Contrasting

Unclassified

Order By: Relevance

“…Preparation of Anti-GCP16 -cDNA encoding a chimeric protein of GCP16 fused to the COOH terminus of glutathione S-transferase (GST) 1 was constructed in expression vector pGEX4T-1 (15) and designated GST-GCP16. The recombinant protein was expressed in and purified from bacteria and injected into rabbits to raise anti-GST-GCP16 antibodies as described previously (15).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Identification and Characterization of GCP16, a Novel Acylated Golgi Protein That Interacts with GCP170

Ohta

Misumi

Sohda

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

GCP170, a member of the golgin family associated with the cytoplasmic face of the Golgi membrane, was found to have a Golgi localization signal at the NH 2 -terminal region (positions 137-237). Using this domain as bait in the yeast two-hybrid screening system, we identified a novel protein that interacted with GCP170. The 2.0-kilobase mRNA encoding a 137-amino acid protein of 16 kDa designated GCP16 was ubiquitously expressed. Immunofluorescence microscopy showed that GCP16 was co-localized with GCP170 and giantin in the Golgi region. Despite the absence of a hydrophobic domain sufficient for participating in membrane localization, GCP16 was found to be tightly associated with membranes like an integral membrane protein. 69 and Cys 72 , accounting for its tight association with the membrane. A mutant without potential acylation sites (C69A/C72A) was no longer localized to the Golgi, indicating that the acylation is prerequisite for the Golgi localization of GCP16. Although the mutant GCP16, even when overexpressed, had no effect on protein transport, overexpression of the wild type GCP16 caused an inhibitory effect on protein transport from the Golgi to the cell surface. Taken together, these results indicate that GCP16 is the acylated membrane protein, associated with GCP170, and possibly involved in vesicular transport from the Golgi to the cell surface. Labeling experiments with [ 3 H]palmitic acid and mutational analysis demonstrated that GCP16 was acylated at Cys

show abstract

Section: Methodsmentioning

confidence: 99%

“…The major functions of Golgi complex are thought to be in processing and sorting of lipids and proteins en route from the endoplasmic reticulum to the plasma membrane and other destinations (1). Various enzymes involved in proteolytic and oligosaccharide processing of the transported proteins are localized to subcompartments of the Golgi complex (1-3).…”

mentioning

confidence: 99%

Identification and Characterization of GCP16, a Novel Acylated Golgi Protein That Interacts with GCP170

Ohta

Misumi

Sohda

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…It is the primary site for sorting and processing of proteins undergoing both exocytosis and endocytosis (reviewed in Farquhar and Palade, 1998). Under normal conditions, the mammalian Golgi complex is a collection of stacks of cisternal membranes near the microtubule organizing center.…”

Section: Introductionmentioning

confidence: 99%

Caspase-resistant Golgin-160 Disrupts Apoptosis Induced by Secretory Pathway Stress and Ligation of Death Receptors

Maag

Mancini

Rosen

et al. 2005

MBoC

View full text Add to dashboard Cite

Golgin-160 is a coiled-coil protein on the cytoplasmic face of the Golgi complex that is cleaved by caspases during apoptosis. We assessed the sensitivity of cell lines stably expressing wild-type or caspase-resistant golgin-160 to several proapoptotic stimuli. Cells expressing a caspase-resistant mutant of golgin-160 were strikingly resistant to apoptosis induced by ligation of death receptors and by drugs that induce endoplasmic reticulum (ER) stress, including brefeldin-A, dithiothreitol, and thapsigargin. However, both cell lines responded similarly to other proapoptotic stimuli, including staurosporine, anisomycin, and etoposide. The caspase-resistant golgin-160 dominantly prevented cleavage of endogenous golgin-160 after ligation of death receptors or induction of ER stress, which could be explained by a failure of initiator caspase activation. The block in apoptosis in cells expressing caspase-resistant golgin-160 could not be bypassed by expression of potential caspase cleavage fragments of golgin-160, or by drug-induced disassembly of the Golgi complex. Our results suggest that some apoptotic signals (including those initiated by death receptors and ER stress) are sensed and integrated at Golgi membranes and that golgin-160 plays an important role in transduction of these signals. INTRODUCTIONThe Golgi complex is central to the regulation of membrane trafficking in eukaryotic cells. It is the primary site for sorting and processing of proteins undergoing both exocytosis and endocytosis (reviewed in Farquhar and Palade, 1998). Under normal conditions, the mammalian Golgi complex is a collection of stacks of cisternal membranes near the microtubule organizing center. Proteins traversing the secretory pathway enter the Golgi at the cis face, are processed as they pass through the Golgi stacks, and are sorted at the trans face into vesicles bound for their intended destinations. The trans-Golgi is also important in sorting proteins being endocytosed or cycling between the plasma membrane and intracellular membrane compartments. This affords the Golgi extensive communication with the rest of the cell and its surroundings, placing it in a prime position to sense and integrate information about the state of the cell and its environment.The structure of the Golgi is highly dynamic, allowing reversible disassembly during mitosis. Key secretory pathway proteins are phosphorylated in a cell cycle-dependent manner to stop membrane trafficking and disassemble the Golgi (reviewed in Rabouille and Jokitalo, 2003). This rearrangement from a single perinuclear organelle to dispersed vesiculated compartments is thought to ensure partitioning of the Golgi complex into both daughter cells during cytokinesis. When Golgi disassembly is prevented by addition of antibodies to Golgi reassembly and stacking protein of 65 kDa (GRASP65), cells complete S phase, but they are unable to enter mitosis. This mitotic block can be bypassed by disassembling the Golgi with drugs (Sutterlin et al., 2002). Once mitosis is complete, the Golgi...

show abstract

“…The Golgi apparatus lies at the heart of the secretory pathway and plays a critical role in the posttranslational modification and trafficking of secretory cargo proteins and lipids (1). In addition to these core functions, the Golgi apparatus also contributes to cell cycle regulation and cytoskeletal dynamics (2)(3)(4).…”

mentioning

confidence: 99%

Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice

Liu

Mei

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

104

View full text Add to dashboard Cite

The Golgi apparatus lies at the heart of the secretory pathway where it is required for secretory trafficking and cargo modification. Disruption of Golgi architecture and function has been widely observed in neurodegenerative disease, but whether Golgi dysfunction is causal with regard to the neurodegenerative process, or is simply a manifestation of neuronal death, remains unclear. Here we report that targeted loss of the golgin GM130 leads to a profound neurological phenotype in mice. Global KO of mouse GM130 results in developmental delay, severe ataxia, and postnatal death. We further show that selective deletion of GM130 in neurons causes fragmentation and defective positioning of the Golgi apparatus, impaired secretory trafficking, and dendritic atrophy in Purkinje cells. These cellular defects manifest as reduced cerebellar size and Purkinje cell number, leading to ataxia. Purkinje cell loss and ataxia first appear during postnatal development but progressively worsen with age. Our data therefore indicate that targeted disruption of the mammalian Golgi apparatus and secretory traffic results in neuronal degeneration in vivo, supporting the view that Golgi dysfunction can play a causative role in neurodegeneration.GM130 | Golgi apparatus | polarized secretion | Purkinje cell | ataxia

show abstract

The Golgi apparatus: 100 years of progress and controversy

Cited by 284 publications

References 88 publications

Identification and Characterization of GCP16, a Novel Acylated Golgi Protein That Interacts with GCP170

Identification and Characterization of GCP16, a Novel Acylated Golgi Protein That Interacts with GCP170

Caspase-resistant Golgin-160 Disrupts Apoptosis Induced by Secretory Pathway Stress and Ligation of Death Receptors

Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice

Contact Info

Product

Resources

About