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Cells Jan 2022Golgi apparatus is the central component of the mammalian secretory pathway and it regulates the biosynthesis of the plasma membrane through three distinct but... (Review)
Review
Golgi apparatus is the central component of the mammalian secretory pathway and it regulates the biosynthesis of the plasma membrane through three distinct but interacting processes: (a) processing of protein and lipid cargoes; (b) creation of a sharp transition in membrane lipid composition by non-vesicular transport of lipids; and (c) vesicular sorting of proteins and lipids at the trans-Golgi network to target them to appropriate compartments. We discuss the molecules involved in these processes and their importance in physiology and development. We also discuss how mutations in these molecules affect plasma membrane composition and signaling leading to genetic diseases and cancer.
Topics: Animals; Cell Membrane; Golgi Apparatus; Mammals; Membrane Lipids; Protein Transport; trans-Golgi Network
PubMed: 35159178
DOI: 10.3390/cells11030368 -
Results and Problems in Cell... 2019The Golgi apparatus is a central intracellular membrane-bound organelle with key functions in trafficking, processing, and sorting of newly synthesized membrane and... (Review)
Review
The Golgi apparatus is a central intracellular membrane-bound organelle with key functions in trafficking, processing, and sorting of newly synthesized membrane and secretory proteins and lipids. To best perform these functions, Golgi membranes form a unique stacked structure. The Golgi structure is dynamic but tightly regulated; it undergoes rapid disassembly and reassembly during the cell cycle of mammalian cells and is disrupted under certain stress and pathological conditions. In the past decade, significant amount of effort has been made to reveal the molecular mechanisms that regulate the Golgi membrane architecture and function. Here we review the major discoveries in the mechanisms of Golgi structure formation, regulation, and alteration in relation to its functions in physiological and pathological conditions to further our understanding of Golgi structure and function in health and diseases.
Topics: Animals; Biological Transport; Cell Cycle; Disease; Golgi Apparatus; Health; Humans; Intracellular Membranes; Stress, Physiological
PubMed: 31435807
DOI: 10.1007/978-3-030-23173-6_19 -
Histochemistry and Cell Biology Oct 2013In 1898, the Golgi apparatus was discovered by light microscopy, and since the 1950s, the ultrastructure composition is known by electron microscopic investigation. The... (Review)
Review
In 1898, the Golgi apparatus was discovered by light microscopy, and since the 1950s, the ultrastructure composition is known by electron microscopic investigation. The complex three-dimensional morphology fascinated researchers and was sometimes even the driving force to develop novel visualization techniques. However, the highly dynamic membrane systems of Golgi apparatus are delicate and prone to fixation artifacts. Therefore, the understanding of Golgi morphology and its function has been improved significantly with the development of better preparation methods. Nowadays, cryo-fixation is the method of choice to arrest instantly all dynamic and physiological processes inside cells, tissues, and small organisms. Embedded in amorphous ice, such samples can be further processed by freeze substitution or directly analyzed in their fully hydrated state by cryo-electron microscopy and tomography. Even though the overall morphology of vitrified Golgi stacks is comparable to well-prepared and resin-embedded samples, previously unknown structural details can be observed solely based on their native density. At this point, any further improvement of sample preparation would gain novel insights, perhaps not in terms of general morphology, but on fine structural details of this dynamic organelle.
Topics: Animals; Cryoelectron Microscopy; Golgi Apparatus; Humans
PubMed: 23954988
DOI: 10.1007/s00418-013-1136-3 -
Traffic (Copenhagen, Denmark) Apr 2012The Golgi apparatus is an organelle that has been extensively studied in the model eukaryote, yeast. Its morphology varies among yeast species; the Golgi exists as a... (Review)
Review
The Golgi apparatus is an organelle that has been extensively studied in the model eukaryote, yeast. Its morphology varies among yeast species; the Golgi exists as a system of dispersed cisternae in the case of the budding yeast Saccharomyces cerevisiae, whereas the Golgi cisternae in Pichia pastoris and Schizosaccharomyces pombe are organized into stacks. In spite of the different organization, the mechanism of trafficking through the Golgi apparatus is believed to be similar, involving cisternal maturation, in which the resident Golgi proteins are transported backwards while secretory cargo proteins can stay in the cisternae. Questions remain regarding the organization of the yeast Golgi, the regulatory mechanisms that underlie cisternal maturation of the Golgi and transport machinery of cargo proteins through this organelle. Studies using different yeast species have provided hints to these mechanisms.
Topics: Biological Transport; Golgi Apparatus; Models, Biological; Saccharomyces cerevisiae; Signal Transduction
PubMed: 22132734
DOI: 10.1111/j.1600-0854.2011.01316.x -
Current Biology : CB Aug 2000
Review
Topics: Animals; Cell Cycle; Endoplasmic Reticulum; Golgi Apparatus; Membrane Proteins; Models, Biological; Protein Transport; SNARE Proteins; Transport Vesicles; Vesicular Transport Proteins
PubMed: 10985372
DOI: 10.1016/s0960-9822(00)00644-8 -
Molecular Biology of the Cell Jul 1998
Topics: Animals; Biological Transport; Brefeldin A; COS Cells; Endoplasmic Reticulum; Golgi Apparatus; Green Fluorescent Proteins; Intracellular Membranes; Light; Luminescent Proteins; Membrane Glycoproteins; Microscopy, Video; Vesicular stomatitis Indiana virus; Video Recording; Viral Envelope Proteins
PubMed: 9658158
DOI: 10.1091/mbc.9.7.1617 -
Archives of Histology and Cytology Aug 2002One hundred years have passed since the discovery of "the internal reticular apparatus" by Camillo GOLGI. Investigations into the structure and function of the "Golgi... (Review)
Review
One hundred years have passed since the discovery of "the internal reticular apparatus" by Camillo GOLGI. Investigations into the structure and function of the "Golgi apparatus" have raised more and more challenging issues for cell biologists. After long debate, many new findings have accumulated in the last 10 years as a result of the availability of elegant new genetic, biochemical and morphological tools. This, in turn, has raised many new questions to be solved. In addition, numerous new findings have led to some confusion on the understanding of the Golgi apparatus. This review article deals with several modern aspects of vesicular transport versus cisternal maturation. Disruption of the stacked structure in mitotic and drug-induced conditions is also discussed to demonstrate the importance of structural integrity in the Golgi apparatus.
Topics: Animals; Brefeldin A; Endoplasmic Reticulum; Golgi Apparatus; Membrane Proteins; Mitosis; Models, Biological; Models, Structural; Okadaic Acid; Transport Vesicles
PubMed: 12389660
DOI: 10.1679/aohc.65.209 -
Molecular Membrane Biology 2003This review discusses the mitotic segregation of the Golgi apparatus. The results from classical biochemical and morphological studies have suggested that in mammalian... (Review)
Review
This review discusses the mitotic segregation of the Golgi apparatus. The results from classical biochemical and morphological studies have suggested that in mammalian cells this organelle remains distinct during mitosis, although highly fragmented through the formation of mitotic Golgi clusters of small tubules and vesicles. Shedding of free Golgi-derived vesicles would consume Golgi clusters and disperse this organelle throughout the cytoplasm. Vesicles could be partitioned in a stochastic and passive way between the two daughter cells and act as a template for the reassembly of this key organelle. This model has recently been modified by results obtained using GFP- or HRP-tagged Golgi resident enzymes, live cell imaging and electron microscopy. Results obtained with these techniques show that the mitotic Golgi clusters are stable entities throughout mitosis that partition in a microtubule spindle-dependent fashion. Furthermore, a newer model proposes that at the onset of mitosis, the Golgi apparatus completely loses its identity and is reabsorbed into the endoplasmic reticulum. This suggests that the partitioning of the Golgi apparatus is entirely dependent on the partitioning of the endoplasmic reticulum. We critically discuss both models and summarize what is known about the molecular mechanisms underlying the Golgi disassembly and reassembly during and after mitosis. We will also review how the study of the Golgi apparatus during mitosis in other organisms can answer current questions and perhaps reveal novel mechanisms.
Topics: Animals; COP-Coated Vesicles; Cell Division; Golgi Apparatus; Humans; Interphase; Microscopy, Electron; Saccharomyces cerevisiae
PubMed: 12851069
DOI: 10.1080/0968768031000084163 -
Journal of Electron Microscopy Technique Feb 1991The ability to radiolabel biological molecules, in conjunction with radioautographic or cell fractionation techniques, has brought about a revolution in our knowledge of... (Review)
Review
The ability to radiolabel biological molecules, in conjunction with radioautographic or cell fractionation techniques, has brought about a revolution in our knowledge of dynamic cellular processes. This has been particularly true since the 1940's, when isotopes such as 35S and 14C became available, since these isotopes could be incorporated into a great variety of biologically important compounds. The first dynamic evidence for Golgi apparatus involvement in biosynthesis came from light microscope radioautographic studies by Jennings and Florey in the 1950's, in which label was localized to the supranuclear Golgi region of goblet cells soon after injection of 35S-sulfate. When the low energy isotope tritium became available, and when radioautography could be extended to the electron microscope level, a great improvement in spatial resolution was achieved. Studies using 3H-amino acids revealed that proteins were synthesized in the rough endoplasmic reticulum, migrated to the Golgi apparatus, and thence to secretion granules, lysosomes, or the plasma membrane. The work of Neutra and Leblond in the 1960's using 3H-glucose provided dramatic evidence that the Golgi apparatus was involved in glycosylation. Work with 3H-mannose (a core sugar in N-linked side chains), showed that this sugar was incorporated into glycoproteins in the rough endoplasmic reticulum, providing the first radioautographic evidence that glycosylation of proteins did not occur solely in the Golgi apparatus. Studies with the tritiated precursors of fucose, galactose, and sialic acid, on the other hand, showed that these terminal sugars are mainly added in the Golgi apparatus. With its limited spatial resolution, radioautography cannot discriminate between label in adjacent Golgi saccules. Nonetheless, in some cell types, radioautographic evidence (along with cytochemical and cell fractionation data) has indicated that the Golgi is subcompartmentalized in terms of glycosylation, with galactose and sialic acid being added to glycoproteins only within the trans-Golgi compartment. In the last ten years, radioautographic tracing of radioiodinated plasma membrane molecules has indicated a substantial recycling of such molecules to the Golgi apparatus.
Topics: Animals; Autoradiography; Biological Transport; Cell Compartmentation; Glycosylation; Golgi Apparatus; Protein Biosynthesis
PubMed: 2013818
DOI: 10.1002/jemt.1060170203 -
The International Journal of... Nov 2012The classical view of the Golgi apparatus is of a small membranous organelle involved in protein transport and secretion. Recent descriptions of the molecular network... (Review)
Review
The classical view of the Golgi apparatus is of a small membranous organelle involved in protein transport and secretion. Recent descriptions of the molecular network connecting the Golgi to other organelles demonstrate the essential roles of the Golgi in cellular activities as a stress sensor, apoptosis trigger, lipid/protein modifier, mitotic checkpoint, and a mediator of malignant transformation. Thus, the Golgi function should have a fundamental impact on cancer cell survival. Prostate cancer is initially responsive to androgenic hormones; however, it almost invariably progresses to a castration-refractory or hormone-insensitive state. Nevertheless, androgen signaling remains active at this stage and is important as a therapeutic target. Certain Golgi-associated molecules have recently been demonstrated to be regulated by androgen action, and the Golgi is emerging as a new therapeutic target in prostate cancer. The key Golgi-associated molecules essential for prostate cancer development and the potential therapeutic options targeting the Golgi apparatus are discussed.
Topics: Antineoplastic Agents; Golgi Apparatus; Humans; Male; Models, Biological; Prostatic Neoplasms
PubMed: 22721754
DOI: 10.1016/j.biocel.2012.06.004