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BioFactors (Oxford, England) Nov 2021The organelle of eukaryotes is a finely regulated system. Once disturbed, it activates the specific autoregulatory systems, namely, organelle autoregulation. Among... (Review)
Review
The organelle of eukaryotes is a finely regulated system. Once disturbed, it activates the specific autoregulatory systems, namely, organelle autoregulation. Among which, the Golgi stress response accounts for one. When the abundance and capacity of the Golgi apparatus are insufficient compared with cellular demand, the Golgi stress response is activated to enhance the function of the Golgi apparatus. Although the molecular mechanism of the Golgi stress response has not been well characterized yet, it seems to be an important part of the mammalian stress response. In this review, we discuss the current status of research on the six pathways of the mammalian Golgi stress response (the TFE3, heat shock protein 47, CREB3, E26 transformation specific, proteoglycan, and mucin pathways), which regulate the general function of the Golgi apparatus, anti-apoptosis, pro-apoptosis, proteoglycan glycosylation, and mucin glycosylation, respectively.
Topics: Golgi Apparatus; HeLa Cells; Homeostasis; Humans; Mucins; Stress, Physiological
PubMed: 34500494
DOI: 10.1002/biof.1780 -
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 -
Methods in Molecular Biology (Clifton,... 2023Immunofluorescence is a technique that uses antibodies and fluorophores to label structures inside cells. The cells are normally fixed and permeabilized, and then...
Immunofluorescence is a technique that uses antibodies and fluorophores to label structures inside cells. The cells are normally fixed and permeabilized, and then structures are labelled using primary antibodies directly conjugated to fluorophores, or, more commonly, first with an antibody against an antigen of interest followed by a secondary antibody conjugated to a fluorophore that binds to the primary antibody. Fluorescence can be visualized using widefield, confocal, or super-resolution microscopy. Here we focus on labelling of the Golgi apparatus and show that different fixation and permeabilization conditions can significantly affect labelling of Golgi proteins and describe how to optimize fluorescent detection of Golgi proteins.
Topics: Animals; Golgi Apparatus; Microscopy, Fluorescence; Fluorescent Antibody Technique; Fluorescent Dyes; Antibodies; Microscopy, Confocal; Mammals
PubMed: 36512212
DOI: 10.1007/978-1-0716-2639-9_8 -
Trends in Cell Biology Jul 2018Microtubule organization has a crucial role in regulating cell architecture. The geometry of microtubule arrays strongly depends on the distribution of sites responsible... (Review)
Review
Microtubule organization has a crucial role in regulating cell architecture. The geometry of microtubule arrays strongly depends on the distribution of sites responsible for microtubule nucleation and minus-end attachment. In cycling animal cells, the centrosome often represents a dominant microtubule-organizing center (MTOC). However, even in cells with a radial microtubule system, many microtubules are not anchored at the centrosome, but are instead linked to the Golgi apparatus or other structures. Non-centrosomal microtubules predominate in many types of differentiated cell and in mitotic spindles. In this review, we discuss recent advances in understanding how the organization of centrosomal and non-centrosomal microtubule networks is controlled by proteins involved in microtubule nucleation and specific factors that recognize free microtubule minus ends and regulate their localization and dynamics.
Topics: Animals; Centrosome; Golgi Apparatus; Humans; Microtubule-Organizing Center; Microtubules
PubMed: 29571882
DOI: 10.1016/j.tcb.2018.02.011 -
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 -
Current Opinion in Cell Biology Apr 2016Over the past few decades, it has emerged that the Golgi (and other secretory stations) is host to a variety of signaling molecules and can act as a signaling hub that... (Review)
Review
Over the past few decades, it has emerged that the Golgi (and other secretory stations) is host to a variety of signaling molecules and can act as a signaling hub that receives, emits and elaborates signals. This endomembrane-based signaling apparatus appears to have more than one purpose. Its most fundamental function appears to be the auto-regulation of the biosynthetic apparatus to maintain and/or optimize its own activities and to coordinate such activities with those of other cellular modules.(1) This is achieved by dedicated control devices that provide stability, robustness, precision, sensitivity and complexity to cellular behaviors.
Topics: Animals; Biological Transport; Cell Membrane; Golgi Apparatus; Humans; Proteins; Signal Transduction
PubMed: 26908115
DOI: 10.1016/j.ceb.2016.01.014 -
International Review of Cell and... 2018The secretory and autophagic pathways are two fundamental, evolutionary highly conserved endomembrane processes. Typically, secretion is associated with biosynthesis and... (Review)
Review
The secretory and autophagic pathways are two fundamental, evolutionary highly conserved endomembrane processes. Typically, secretion is associated with biosynthesis and delivery of proteins. In contrast, autophagy is usually considered as a degradative pathway. Thus, an analogy to metabolic pathways is evident. Anabolic (biosynthetic) and catabolic (degradative) pathways are usually intimately linked and intertwined, and likewise, the secretory and autophagy pathways are intertwined. Investigation of this link is an emerging area of research, and we will provide an overview of some of the major advances that have been made to contribute to understanding of how secretion regulates autophagy and vice versa. Finally, we will highlight evidence that supports a potential involvement of the autophagy-secretion crosstalk in human diseases.
Topics: Autophagy; Disease; Endoplasmic Reticulum; Golgi Apparatus; Humans; Secretory Pathway
PubMed: 29551160
DOI: 10.1016/bs.ircmb.2017.12.004 -
FEBS Letters Sep 2019
Topics: Biological Transport; Golgi Apparatus; Homeostasis; Lipids; Signal Transduction
PubMed: 31495944
DOI: 10.1002/1873-3468.13577 -
Methods in Molecular Biology (Clifton,... 2023Maintaining protein homeostasis (proteostasis) is vital to cellular and organismal health. How the Golgi apparatus, the central protein maturation and sorting station in...
Maintaining protein homeostasis (proteostasis) is vital to cellular and organismal health. How the Golgi apparatus, the central protein maturation and sorting station in the cell, manages misfolded proteins to maintain proteostasis is still poorly understood. Here we present a strategy for targeted protein unfolding at the Golgi that enables studying Golgi-related protein quality control and stress-signaling pathways. Targeted protein unfolding is induced by small molecule-based chemical biology approaches-hydrophobic tagging and the use of a destabilization domain. Imaging studies allow visualizing quality control (QC) phenotypes, such as the formation of QC carriers and Golgi-to-endoplasmic reticulum trafficking, and correlating these phenotypes with other trafficking processes.
Topics: Golgi Apparatus; Endoplasmic Reticulum; Protein Transport; Protein Unfolding
PubMed: 36512243
DOI: 10.1007/978-1-0716-2639-9_39 -
FEBS Letters Sep 2019Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are lipid APs attached to the extracellular leaflet of the plasma membrane (PM) via a glycolipid anchor. GPI-APs... (Review)
Review
Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are lipid APs attached to the extracellular leaflet of the plasma membrane (PM) via a glycolipid anchor. GPI-APs are commonly associated with cholesterol- and sphingolipid-enriched membrane microdomains. These microdomains help regulating various biological activities, by segregating different proteins and lipids in (nanoscale) membrane compartments. In fibroblasts, GPI-APs form actin- and cholesterol-dependent nanoclusters directly at the PM. In contrast, in polarized epithelial cells GPI-APs cluster in the Golgi apparatus, the major protein-sorting hub for the secretory pathway. Golgi clustering is required for the selective sorting of GPI-APs to the apical PM domain, but also regulates their organization and biological activities at the cell surface. In this review, we discuss recent advances in our understanding of the mechanism of GPI-AP sorting to the apical membrane. We focus on the roles of the protein moiety and lipids in the regulation of the clustering of GPI-APs in the Golgi apparatus.
Topics: Animals; Epithelial Cells; Golgi Apparatus; Humans; Membrane Proteins; Protein Transport
PubMed: 31400147
DOI: 10.1002/1873-3468.13573