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Proceedings of the National Academy of... May 2017The Golgi apparatus is a membrane-bounded organelle with the characteristic shape of a series of stacked flat cisternae. During mitosis in mammalian cells, the Golgi...
The Golgi apparatus is a membrane-bounded organelle with the characteristic shape of a series of stacked flat cisternae. During mitosis in mammalian cells, the Golgi apparatus is once fragmented into small vesicles and then reassembled to form the characteristic shape again in each daughter cell. The mechanism and details of the reassembly process remain elusive. Here, by the physical simulation of a coarse-grained membrane model, we reconstructed the three-dimensional morphological dynamics of the Golgi reassembly process. Considering the stability of the interphase Golgi shape, we introduce two hypothetical mechanisms-the Golgi rim stabilizer protein and curvature-dependent restriction on membrane fusion-into the general biomembrane model. We show that the characteristic Golgi shape is spontaneously organized from the assembly of vesicles by proper tuning of the two additional mechanisms, i.e., the Golgi reassembly process is modeled as self-organization. We also demonstrate that the fine Golgi shape forms via a balance of three reaction speeds: vesicle aggregation, membrane fusion, and shape relaxation. Moreover, the membrane fusion activity decreases thickness and the number of stacked cisternae of the emerging shapes.
Topics: Animals; Computer Simulation; Golgi Apparatus; Humans; Membrane Fusion; Mitosis; Models, Biological; Protein Stability
PubMed: 28461510
DOI: 10.1073/pnas.1619264114 -
Science (New York, N.Y.) Feb 1972
Review
Topics: Biological Transport; Carbohydrates; Cell Membrane; Glucosyltransferases; Glycoproteins; Golgi Apparatus; Lysosomes; Macromolecular Substances; Polysaccharides
PubMed: 4550618
DOI: 10.1126/science.175.4022.596 -
Cold Spring Harbor Perspectives in... Oct 2011The Golgi is an essential membrane-bound organelle in the secretary pathway of eukaryotic cells. In mammalian cells, the Golgi stacks are integrated into a continuous... (Review)
Review
The Golgi is an essential membrane-bound organelle in the secretary pathway of eukaryotic cells. In mammalian cells, the Golgi stacks are integrated into a continuous perinuclear ribbon, which poses a challenge for the daughter cells to inherit this membrane organelle during cell division. To facilitate proper partitioning, the mammalian Golgi ribbon is disassembled into vesicles in early mitosis. Following segregation into the daughter cells, a functional Golgi is reformed. Here we summarize our current understanding of the molecular mechanisms that control the mitotic Golgi disassembly and postmitotic reassembly cycle in mammalian cells.
Topics: Animals; Golgi Apparatus; Mammals; Membrane Fusion; Mitosis
PubMed: 21690214
DOI: 10.1101/cshperspect.a005330 -
Cold Spring Harbor Perspectives in... Apr 2011Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to... (Review)
Review
Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to glycoproteins or glycolipids occurs in the ER or on the ER membrane, the subsequent addition of the many different sugars that make up a mature glycan is accomplished in the Golgi. Golgi membranes are studded with glycosyltransferases, glycosidases, and nucleotide sugar transporters arrayed in a generally ordered manner from the cis-Golgi to the trans-Golgi network (TGN), such that each activity is able to act on specific substrate(s) generated earlier in the pathway. The spectrum of glycosyltransferases and other activities that effect glycosylation may vary with cell type, and thus the final complement of glycans on glycoconjugates is variable. In addition, glycan synthesis is affected by Golgi pH, the integrity of Golgi peripheral membrane proteins, growth factor signaling, Golgi membrane dynamics, and cellular stress. Knowledge of Golgi glycosylation has fostered the development of assays to identify mechanisms of intracellular vesicular trafficking and facilitated glycosylation engineering of recombinant glycoproteins.
Topics: Endoplasmic Reticulum; Glycosylation; Golgi Apparatus; Lipid Metabolism; Proteins; Signal Transduction
PubMed: 21441588
DOI: 10.1101/cshperspect.a005199 -
Biochemical Society Symposium 2005Protein kinases control Golgi function in both mitotic and interphase cells. In mitosis, phosphorylation of structural proteins by Cdk1 (cyclin-dependent kinase... (Review)
Review
Protein kinases control Golgi function in both mitotic and interphase cells. In mitosis, phosphorylation of structural proteins by Cdk1 (cyclin-dependent kinase 1)-cyclin B, Polo-like and mitogen-activated protein kinases underlie changes in Golgi reorganization during cell division. While in interphase, signalling pathways that are associated with the Golgi control secretory function through a variety of mechanisms. Some of these, notably those involving protein kinase D and Ste20 family kinases, are also relevant for the establishment and maintenance of cell polarization and migration.
Topics: Animals; Cell Movement; Cell Polarity; Golgi Apparatus; Humans; Interphase; Mitosis; Protein Kinases; Signal Transduction
PubMed: 15649126
DOI: 10.1042/bss0720015 -
Current Opinion in Cell Biology Aug 2010There are, in theory, several ways in which proteins may pass through the Golgi apparatus. Among these, the cisternal progression-maturation mode has gained broad... (Review)
Review
There are, in theory, several ways in which proteins may pass through the Golgi apparatus. Among these, the cisternal progression-maturation mode has gained broad consensus. However, there remain questions regarding the molecular mechanisms by which resident proteins are sorted from cargo and move backward to the proximal cisterna in synchrony with cisternal progression. In this short review, we discuss current questions about the organisation of trafficking to, through, and out of the Golgi apparatus, as well as the main approaches being developed to address such questions in model organisms including yeast, mammals and plants.
Topics: Animals; Endoplasmic Reticulum; Golgi Apparatus; Humans; Models, Biological; Protein Transport; trans-Golgi Network
PubMed: 20605430
DOI: 10.1016/j.ceb.2010.05.003 -
Current Opinion in Cell Biology Aug 1998The past year has seen considerable progress in understanding the mechanism of COPI (coatomer protein I) vesicle docking and SNARE (soluble NSF attachment protein... (Review)
Review
The past year has seen considerable progress in understanding the mechanism of COPI (coatomer protein I) vesicle docking and SNARE (soluble NSF attachment protein receptor) mediated fusion, the mechanism of cisternal growth and stacking and the regulation of Golgi architecture. The route taken by cargo proteins through the Golgi apparatus is still a matter of some dispute.
Topics: Animals; Golgi Apparatus; Humans
PubMed: 9719870
DOI: 10.1016/s0955-0674(98)80064-1 -
The Journal of Histochemistry and... Jul 1982Its topography is one of the most characteristic features of the Golgi apparatus and the reticular nature of this organelle is evident in Golgi's first drawings, in... (Review)
Review
The internal reticular apparatus of Camillo Golgi: a complex, heterogeneous organelle, enriched in acid, neutral, and alkaline phosphatases, and involved in glycosylation, secretion, membrane flow, lysosome formation, and intracellular digestion.
Its topography is one of the most characteristic features of the Golgi apparatus and the reticular nature of this organelle is evident in Golgi's first drawings, in light microscopic enzyme cytochemical preparations, and in high voltage electron micrographs of thick sections. Although individual components of the Golgi apparatus may differ in staining characteristics, morphology, contents, and enzymatic activities, they are integrated into a dynamic topographical and functional unit that is closely associated with the endoplasmic reticulum. Modulation of enzymatic activities and morphological and enzymatic heterogeneity are not surprising in an organelle that is the site of both synthetic and digestive events, including glycosylation, sulfation, formation of secretory granules and lysosomes, and the degradation of endocytized material.
Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Biological Transport; Golgi Apparatus; Histocytochemistry; Lysosomes; Microscopy, Electron; Phosphoric Monoester Hydrolases; Rats
PubMed: 6286754
DOI: 10.1177/30.7.6286754 -
The American Journal of Pathology Oct 1994The importance of the Golgi apparatus in the transport, processing, and targeting of proteins destined for secretion, plasma membranes, and lysosomes has emerged from... (Review)
Review
The importance of the Golgi apparatus in the transport, processing, and targeting of proteins destined for secretion, plasma membranes, and lysosomes has emerged from numerous studies. In this paper we review studies from our laboratory dealing with 1) the Golgi apparatus during mitosis and the role of microtubules in maintaining the structure of the organelle, 2) the endocytosis of antibodies, exogenous lectins, and toxins into the Golgi apparatus of several cells including neurons in vivo and in vitro, 3) the traffic of MG-160, a membrane sialoglycoprotein of the medial cisternae of the Golgi apparatus, from the trans-Golgi network to the Golgi cisternae, and 4) the involvement of the Golgi apparatus of motor neurons in the pathogenesis of amyotrophic lateral sclerosis. We conclude with a summary of ongoing work on the primary structure of MG-160 and introduce evidence suggesting that this intrinsic membrane protein of the Golgi apparatus may be involved in the regulation of endogenous, autocrine, basic fibroblast growth factor. We hope that this review will stimulate studies on the Golgi apparatus of neurons, which may lead to the discovery of neuron-specific properties of this important organelle and its involvement in the pathogenesis of neurodegenerative disorders.
Topics: Amyotrophic Lateral Sclerosis; Animals; Antibodies; Endocytosis; Golgi Apparatus; Humans; Lectins; Microtubules; Mitosis; Motor Neurons; Organelles; Receptors, Cell Surface; Receptors, Fibroblast Growth Factor; Sialoglycoproteins; Toxins, Biological
PubMed: 7943166
DOI: No ID Found -
FEBS Letters Dec 2009The study of glycosylation and glycosylation enzymes has been instrumental for the advancement of Cell Biology. After Neutra and Leblond showed that the Golgi apparatus... (Review)
Review
The study of glycosylation and glycosylation enzymes has been instrumental for the advancement of Cell Biology. After Neutra and Leblond showed that the Golgi apparatus is the main site of glycosylation, elucidation of oligosaccharide structures by Baenziger and Kornfeld and subsequent mapping of glycosylation enzymes followed. This enabled development of anin vitrotransport assay by Rothman and co-workers using glycosylation to monitor intra Golgi transport which, complemented by yeast genetics by Schekman and co-workers, provided much of the fundamental insights and key components of the secretory pathway that we today take for granted. Glycobiology continues to play a key role in Cell Biology and here, we look at the use of glycosylation enzymes to elucidate intra Golgi transport.
Topics: Animals; Glycosylation; Golgi Apparatus; Humans; Substrate Specificity
PubMed: 19878678
DOI: 10.1016/j.febslet.2009.10.064