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Trends in Cell Biology Jan 1998Research on the Golgi apparatus has resulted in major advances in understanding its structure and functions, but many important questions remain unanswered. The history... (Review)
Review
Research on the Golgi apparatus has resulted in major advances in understanding its structure and functions, but many important questions remain unanswered. The history of the Golgi apparatus has been marked by arguments and controversies, some of which have been resolved, whereas others are still ongoing. This article charts progress in understanding the role of the Golgi apparatus during the 100 years since it was discovered, highlighting major milestones and discoveries that have led to the concepts of the organization and functions of this organelle that we have today.
Topics: Animals; Cell Biology; Golgi Apparatus; History, 19th Century; History, 20th Century; Humans; Italy
PubMed: 9695800
DOI: 10.1016/s0962-8924(97)01187-2 -
Angewandte Chemie (International Ed. in... Jun 2021Changing an oxygen atom of the phosphoester bond in phosphopeptides by a sulfur atom enables instantly targeting Golgi apparatus (GA) and selectively killing cancer...
Changing an oxygen atom of the phosphoester bond in phosphopeptides by a sulfur atom enables instantly targeting Golgi apparatus (GA) and selectively killing cancer cells by enzymatic self-assembly. Specifically, conjugating cysteamine S-phosphate to the C-terminal of a self-assembling peptide generates a thiophosphopeptide. Being a substrate of alkaline phosphatase (ALP), the thiophosphopeptide undergoes rapid ALP-catalyzed dephosphorylation to form a thiopeptide that self-assembles. The thiophosphopeptide enters cells via caveolin-mediated endocytosis and macropinocytosis and instantly accumulates in GA because of dephosphorylation and formation of disulfide bonds in Golgi by themselves and with Golgi proteins. Moreover, the thiophosphopeptide potently and selectively inhibits cancer cells (HeLa) with the IC (about 3 μM), which is an order of magnitude more potent than that of the parent phosphopeptide.
Topics: Alkaline Phosphatase; Golgi Apparatus; HeLa Cells; Humans; Molecular Structure; Peptides; Phosphates
PubMed: 33783926
DOI: 10.1002/anie.202102601 -
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 -
Biochimica Et Biophysica Acta. General... Nov 2020The Conserved Oligomeric Golgi (COG) complex, a multi-subunit vesicle tethering complex of the CATCHR (Complexes Associated with Tethering Containing Helical Rods)... (Review)
Review
The Conserved Oligomeric Golgi (COG) complex, a multi-subunit vesicle tethering complex of the CATCHR (Complexes Associated with Tethering Containing Helical Rods) family, controls several aspects of cellular homeostasis by orchestrating retrograde vesicle traffic within the Golgi. The COG complex interacts with all key players regulating intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. In cells, COG deficiencies result in the accumulation of non-tethered COG-complex dependent (CCD) vesicles, dramatic morphological and functional abnormalities of the Golgi and endosomes, severe defects in N- and O- glycosylation, Golgi retrograde trafficking, sorting and protein secretion. In humans, COG mutations lead to severe multi-systemic diseases known as COG-Congenital Disorders of Glycosylation (COG-CDG). In this report, we review the current knowledge of the COG complex and analyze COG-related trafficking and glycosylation defects in COG-CDG patients.
Topics: Adaptor Proteins, Vesicular Transport; Animals; Biological Transport; Congenital Disorders of Glycosylation; Glycosylation; Golgi Apparatus; Humans; Multiprotein Complexes; Mutation; Protein Interaction Maps; Protein Subunits
PubMed: 32730773
DOI: 10.1016/j.bbagen.2020.129694 -
Journal of Molecular Biology Aug 2016Glycosylation is a ubiquitous modification that occurs on proteins and lipids in all living cells. Consistent with their high complexity, glycans play crucial biological... (Review)
Review
Glycosylation is a ubiquitous modification that occurs on proteins and lipids in all living cells. Consistent with their high complexity, glycans play crucial biological roles in protein quality control and recognition events. Asparagine-linked protein N-glycosylation, the most complex glycosylation, initiates in the endoplasmic reticulum and matures in the Golgi apparatus. This process not only requires an accurate distribution of processing machineries, such as glycosyltransferases, glycosidases, and nucleotide sugar transporters, but also needs an efficient and well-organized factory that is responsible for the fidelity and quality control of sugar chain processing. In addition, accurate glycosylation must occur in coordination with protein trafficking and sorting. These activities are carried out by the Golgi apparatus, a membrane organelle in the center of the secretory pathway. To accomplish these tasks, the Golgi has developed into a unique stacked structure of closely aligned, flattened cisternae in which Golgi enzymes reside; in mammalian cells, dozens of Golgi stacks are often laterally linked into a ribbon-like structure. Here, we review our current knowledge of how the Golgi structure is formed and why its formation is required for accurate glycosylation, with the focus on how the Golgi stacking factors GRASP55 and GRASP65 generate the Golgi structure and how the conserved oligomeric Golgi complex maintains Golgi enzymes in different Golgi subcompartments by retrograde protein trafficking.
Topics: Animals; Biological Transport; Endoplasmic Reticulum; Glycosylation; Golgi Apparatus; Humans; Membrane Proteins; Protein Transport
PubMed: 26956395
DOI: 10.1016/j.jmb.2016.02.030 -
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 -
FEBS Letters Sep 2019
Topics: Biological Transport; Golgi Apparatus; Homeostasis; Lipids; Signal Transduction
PubMed: 31495944
DOI: 10.1002/1873-3468.13577 -
ELife Mar 2024Cargo traffic through the Golgi apparatus is mediated by cisternal maturation, but it remains largely unclear how the -cisternae, the earliest Golgi sub-compartment, is...
Cargo traffic through the Golgi apparatus is mediated by cisternal maturation, but it remains largely unclear how the -cisternae, the earliest Golgi sub-compartment, is generated and how the Golgi matures into the -Golgi network (TGN). Here, we use high-speed and high-resolution confocal microscopy to analyze the spatiotemporal dynamics of a diverse set of proteins that reside in and around the Golgi in budding yeast. We find many mobile punctate structures that harbor yeast counterparts of mammalian endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) proteins, which we term 'yeast ERGIC'. It occasionally exhibits approach and contact behavior toward the ER exit sites and gradually matures into the -Golgi. Upon treatment with the Golgi-disrupting agent brefeldin A, the ERGIC proteins form larger aggregates corresponding to the Golgi entry core compartment in plants, while - and medial-Golgi proteins are absorbed into the ER. We further analyze the dynamics of several late Golgi proteins to better understand the Golgi-TGN transition. Together with our previous studies, we demonstrate a detailed spatiotemporal profile of the entire cisternal maturation process from the ERGIC to the Golgi and further to the TGN.
Topics: Animals; Saccharomyces cerevisiae; Saccharomycetales; Golgi Apparatus; trans-Golgi Network; Endoplasmic Reticulum; Mammals
PubMed: 38501165
DOI: 10.7554/eLife.92900 -
Bioscience Reports May 2022Lysosomes are key regulators of many fundamental cellular processes such as metabolism, autophagy, immune response, cell signalling and plasma membrane repair. These... (Review)
Review
Lysosomes are key regulators of many fundamental cellular processes such as metabolism, autophagy, immune response, cell signalling and plasma membrane repair. These highly dynamic organelles are composed of various membrane and soluble proteins, which are essential for their proper functioning. The soluble proteins include numerous proteases, glycosidases and other hydrolases, along with activators, required for catabolism. The correct sorting of soluble lysosomal proteins is crucial to ensure the proper functioning of lysosomes and is achieved through the coordinated effort of many sorting receptors, resident ER and Golgi proteins, and several cytosolic components. Mutations in a number of proteins involved in sorting soluble proteins to lysosomes result in human disease. These can range from rare diseases such as lysosome storage disorders, to more prevalent ones, such as Alzheimer's disease, Parkinson's disease and others, including rare neurodegenerative diseases that affect children. In this review, we discuss the mechanisms that regulate the sorting of soluble proteins to lysosomes and highlight the effects of mutations in this pathway that cause human disease. More precisely, we will review the route taken by soluble lysosomal proteins from their translation into the ER, their maturation along the Golgi apparatus, and sorting at the trans-Golgi network. We will also highlight the effects of mutations in this pathway that cause human disease.
Topics: Child; Golgi Apparatus; Humans; Lysosomes; Protein Transport; Proteins
PubMed: 35394021
DOI: 10.1042/BSR20211856 -
Cell and Tissue Research Jun 2011The eukaryotic Golgi apparatus is characterized by a stack of flattened cisternae that are surrounded by transport vesicles. The organization and function of the Golgi... (Review)
Review
The eukaryotic Golgi apparatus is characterized by a stack of flattened cisternae that are surrounded by transport vesicles. The organization and function of the Golgi require Golgi matrix proteins, including GRASPs and golgins, which exist primarily as fiber-like bridges between Golgi cisternae or between cisternae and vesicles. In this review, we highlight recent findings on Golgi matrix proteins, including their roles in maintaining the Golgi structure, vesicle tethering, and novel, unexpected functions. These new discoveries further our understanding of the molecular mechanisms that maintain the structure and the function of the Golgi, as well as its relationship with other cellular organelles such as the centrosome.
Topics: Animals; Golgi Apparatus; Humans
PubMed: 21494806
DOI: 10.1007/s00441-011-1166-x