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Trends in Cell Biology Jan 1998Most of the biosynthetic reactions that generate the oligosaccharide structures of eukaryotic cells occur in compartments of the Golgi apparatus. This article provides a... (Review)
Review
Most of the biosynthetic reactions that generate the oligosaccharide structures of eukaryotic cells occur in compartments of the Golgi apparatus. This article provides a brief outline of the major glycosylation pathways of the Golgi, and discusses current understanding of the many factors that can control the glycosylation potential of this organelle. Old and new approaches towards elucidating the organization of glycosylation machinery in the Golgi are also considered.
Topics: Animals; Carbohydrate Sequence; Glycosylation; Golgi Apparatus; Humans; Models, Molecular; Oligosaccharides; Polysaccharides
PubMed: 9695806
DOI: 10.1016/s0962-8924(97)01198-7 -
Cell Structure and Function Jul 1984
Review
Topics: Animals; Endoplasmic Reticulum; Golgi Apparatus
PubMed: 6383632
DOI: 10.1247/csf.9.supplement_s35 -
Seikagaku. the Journal of Japanese... Apr 2017
Review
Topics: Animals; Gene Expression Regulation; Golgi Apparatus; Lysosomes; Peroxisomes; Signal Transduction; Stress, Physiological
PubMed: 29624977
DOI: No ID Found -
Journal of Electron Microscopy Technique Feb 1991This review summarizes data on the distribution of certain glycosylation steps in the Golgi apparatus as revealed by immunolabeling and lectin techniques. The methodical... (Review)
Review
This review summarizes data on the distribution of certain glycosylation steps in the Golgi apparatus as revealed by immunolabeling and lectin techniques. The methodical basis for such investigations was provided by the introduction of the colloidal gold marker system for immunolabeling and the development of new means of tissue processing such as the low-temperature embedding technique using Lowicryl K4M. The application of these techniques together with highly specific antibodies has provided much of the basis for our current understanding of the Golgi apparatus in functional terms. Thus, in many cell types, three Golgi apparatus compartments can be distinguished, whereas in others no such functional subdivision is evident. Investigations on sialyltransferase distribution have also provided direct evidence that GERL is structurally and functionally part of the Golgi apparatus.
Topics: Animals; Galactosyltransferases; Glucosyltransferases; Glycosylation; Golgi Apparatus; Histocytochemistry; Humans; Immunohistochemistry; Lectins; N-Acetylglucosaminyltransferases; Protein Processing, Post-Translational; Sialyltransferases
PubMed: 1826523
DOI: 10.1002/jemt.1060170202 -
Biochimica Et Biophysica Acta Jul 2005In this review we will focus on the recent advances in how coiled-coil proteins of the golgin family give identity and structure to the Golgi apparatus in animal cells.... (Review)
Review
In this review we will focus on the recent advances in how coiled-coil proteins of the golgin family give identity and structure to the Golgi apparatus in animal cells. A number of recent studies reveal a common theme for the targeting of golgins containing the ARL-binding GRIP domain, and the related ARF-binding GRAB domain. Similarly, other golgins such as the vesicle tethering factor p115 and Bicaudal-D are targeted by the Rab GTPases, Rab1 and Rab6, respectively. Together golgins and their regulatory GTPases form a complex network, commonly known as the Golgi matrix, which organizes Golgi membranes and regulates membrane trafficking.
Topics: Animals; Apoptosis; Cytoskeleton; Golgi Apparatus; Membrane Proteins; Mitosis; rab GTP-Binding Proteins
PubMed: 15979508
DOI: 10.1016/j.bbamcr.2005.02.001 -
Clinical Orthopaedics and Related... 1968
Review
Topics: Autoradiography; Biological Transport; Bone Development; Bone and Bones; Cartilage; Cell Membrane; Golgi Apparatus; Humans; Lysosomes; Microscopy, Electron; Minerals; Osteoblasts; Osteoclasts; Osteocytes; Polysaccharides; Protein Biosynthesis
PubMed: 4877096
DOI: No ID Found -
Advances in Anatomy, Embryology, and... 1987
Review
Topics: Animals; Cytoplasmic Granules; Endocytosis; Endoplasmic Reticulum; Female; Golgi Apparatus; Histocytochemistry; Mitosis; Rats
PubMed: 3318283
DOI: 10.1007/978-3-642-72826-6 -
Cold Spring Harbor Perspectives in... Jul 2011Since its first visualization in 1898, the Golgi has been a topic of intense morphological research. A typical mammalian Golgi consists of a pile of stapled cisternae,... (Review)
Review
Since its first visualization in 1898, the Golgi has been a topic of intense morphological research. A typical mammalian Golgi consists of a pile of stapled cisternae, the Golgi stack, which is a key station for modification of newly synthesized proteins and lipids. Distinct stacks are interconnected by tubules to form the Golgi ribbon. At the entrance site of the Golgi, the cis-Golgi, vesicular tubular clusters (VTCs) form the intermediate between the endoplasmic reticulum and the Golgi stack. At the exit site of the Golgi, the trans-Golgi, the trans-Golgi network (TGN) is the major site of sorting proteins to distinct cellular locations. Golgi functioning can only be understood in light of its complex architecture, as was revealed by a range of distinct electron microscopy (EM) approaches. In this article, a general concept of mammalian Golgi architecture, including VTCs and the TGN, is described.
Topics: Animals; COP-Coated Vesicles; Endoplasmic Reticulum; Golgi Apparatus; Humans; Mammals; Mice; Microscopy, Electron; trans-Golgi Network
PubMed: 21502307
DOI: 10.1101/cshperspect.a005181 -
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 -
Cell Motility and the Cytoskeleton 1990