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Current Opinion in Cell Biology Aug 2012The Golgi apparatus is essential for post-translational modifications and sorting of proteins in the secretory pathway. In addition, it further performs a broad range of... (Review)
Review
The Golgi apparatus is essential for post-translational modifications and sorting of proteins in the secretory pathway. In addition, it further performs a broad range of specialized functions. This functional diversity is achieved by combining basic morphological modules of cisternae into higher ordered structures. Linking cisternae into stacks that are further connected through tubules into a continuous Golgi ribbon greatly increases its efficiency and expands its repertoire of functions. During cell division, the different modules of the Golgi are inherited by different mechanisms to maintain its functional and morphological composition.
Topics: Animals; Golgi Apparatus; Mammals
PubMed: 22726585
DOI: 10.1016/j.ceb.2012.05.009 -
Histochemistry and Cell Biology Sep 2013The Golgi apparatus contains multiple classes of cisternae that differ in structure, composition, and function, but there is no consensus about the number and definition... (Review)
Review
The Golgi apparatus contains multiple classes of cisternae that differ in structure, composition, and function, but there is no consensus about the number and definition of these classes. A useful way to classify Golgi cisternae is according to the trafficking pathways by which the cisternae import and export components. By this criterion, we propose that Golgi cisternae can be divided into three classes that correspond to functional stages of maturation. First, cisternae at the cisternal assembly stage receive COPII vesicles from the ER and recycle components to the ER in COPI vesicles. At this stage, new cisternae are generated. Second, cisternae at the carbohydrate synthesis stage exchange material with one another via COPI vesicles. At this stage, most of the glycosylation and polysaccharide synthesis reactions occur. Third, cisternae at the carrier formation stage produce clathrin-coated vesicles and exchange material with endosomes. At this stage, biosynthetic cargo proteins are packaged into various transport carriers, and the cisternae ultimately disassemble. Discrete transitions occur as a cisterna matures from one stage to the next. Within each stage, the structure and composition of a cisterna can evolve, but the trafficking pathways remain unchanged. This model offers a unified framework for understanding the properties of the Golgi in diverse organisms.
Topics: Animals; Biological Transport; Endoplasmic Reticulum; Glycosylation; Golgi Apparatus; Models, Biological; Polysaccharides
PubMed: 23881164
DOI: 10.1007/s00418-013-1128-3 -
FEBS Letters Dec 2009Often considered a defining eukaryotic feature, the Golgi body is one of the most recognizable and functionally integrated cellular organelles. It is therefore... (Review)
Review
Often considered a defining eukaryotic feature, the Golgi body is one of the most recognizable and functionally integrated cellular organelles. It is therefore surprising that some unicellular eukaryotes do not, at first glance, appear to possess Golgi stacks. Here we review the molecular evolutionary, genomic and cell biological evidence for Golgi bodies in these organisms, with the organelle likely present in some form in all cases. This, along with the overwhelming prevalence of stacked cisternae in most eukaryotes, implies that the ancestral eukaryote possessed a stacked Golgi body, with at least eight independent instances of Golgi unstacking in our cellular history.
Topics: Animals; Biological Evolution; Eukaryotic Cells; Genome; Golgi Apparatus; Humans
PubMed: 19837068
DOI: 10.1016/j.febslet.2009.10.025 -
Histochemistry and Cell Biology 1998The proteins that reside in the Golgi carry out functions associated with post-translational modifications, including glycosylation and proteolytic processing, membrane... (Review)
Review
The proteins that reside in the Golgi carry out functions associated with post-translational modifications, including glycosylation and proteolytic processing, membrane transport, recycling of endoplasmic reticulum proteins and maintenance of the structural organisation of the organelle itself. The latter includes Golgi stacking, interconnections between stacks and the microtubule-dependent positioning of the organelle within the cell. There are a number of distinct groups of Golgi membrane proteins, including glycosyltransferases, recycling trans-Golgi network (TGN) proteins, peripheral membrane proteins and receptors. Considerable effort has been directed at understanding the basis of the localisation of Golgi glycosyltransferases and recycling TGN proteins; in both cases there is increasing evidence that multiple signals may be involved in their specific localisation. A number of models for the Golgi retention of glycosyltransferases have been proposed including oligomerisation, lipid-mediated sorting and intra-Golgi retrograde transport. More information is required to determine the contribution of each of these potential mechanisms in the targeting of different glycosyltransferases. Future work is also likely to focus on the relationship between the localisation of resident Golgi proteins and the maintenance of Golgi structure.
Topics: Animals; Golgi Apparatus; Humans; Protein Biosynthesis; Protein Processing, Post-Translational; Proteins
PubMed: 9681632
DOI: 10.1007/s004180050252 -
Biochimica Et Biophysica Acta Jul 2005The plant Golgi apparatus is composed of many separate stacks of cisternae which are often associated with the endoplasmic reticulum and which in many cell types are... (Review)
Review
The plant Golgi apparatus is composed of many separate stacks of cisternae which are often associated with the endoplasmic reticulum and which in many cell types are motile. In this review, we discuss the latest data on the molecular regulation of Golgi function. The concept of the Golgi as a distinct organelle is challenged and the possibility of a continuum between the endoplasmic reticulum and Golgi is proposed.
Topics: COP-Coated Vesicles; Endoplasmic Reticulum; Golgi Apparatus; Intracellular Membranes; Models, Biological; Plant Physiological Phenomena; Plant Proteins; Plants; Protein Transport; trans-Golgi Network
PubMed: 16038054
DOI: 10.1016/j.bbamcr.2005.06.006 -
Current Biology : CB Sep 1998
Topics: Animals; Biology; Blood Vessels; Golgi Apparatus; History, 19th Century; History, 20th Century; Italy; Neuroglia; Nobel Prize
PubMed: 9740810
DOI: 10.1016/s0960-9822(07)00407-1 -
FEBS Letters Dec 2009Plant Golgi bodies possess unique morphological and functional characteristics that are key to several biological and biotechnological processes, such as transport of... (Review)
Review
Plant Golgi bodies possess unique morphological and functional characteristics that are key to several biological and biotechnological processes, such as transport of the cell's building blocks to energy-rich compartments, including chloroplasts, storage vacuoles and a cellulosic cell wall. During the last decade it has become apparent that the plant Golgi apparatus has features that are remarkably different from other systems. Here we summarize the most recent findings on this organelle and we highlight pressing questions that are likely to drive the next 10 years of research on the plant Golgi apparatus.
Topics: Cell Division; Endoplasmic Reticulum; Golgi Apparatus; Plant Cells; Plant Proteins; Plants
PubMed: 19800330
DOI: 10.1016/j.febslet.2009.09.046 -
Science Signaling Mar 2024Activation of the endoplasmic reticulum (ER)-resident adaptor protein STING, a component of a cytosolic DNA-sensing pathway, induces the transcription of genes encoding...
Activation of the endoplasmic reticulum (ER)-resident adaptor protein STING, a component of a cytosolic DNA-sensing pathway, induces the transcription of genes encoding type I interferons (IFNs) and other proinflammatory factors. Because STING is activated at the Golgi apparatus, control of the localization and activation of STING is important in stimulating antiviral and antitumor immune responses. Through a genome-wide CRISPR interference screen, we found that STING activation required the Golgi-resident protein ACBD3, which promotes the generation of phosphatidylinositol 4-phosphate (PI4P) at the trans-Golgi network, as well as other PI4P-associated proteins. Appropriate localization and activation of STING at the Golgi apparatus required ACBD3 and the PI4P-generating kinase PI4KB. In contrast, STING activation was enhanced when the lipid-shuttling protein OSBP, which removes PI4P from the Golgi apparatus, was inhibited by the US Food and Drug Administration-approved antifungal itraconazole. The increase in the abundance of STING-activating phospholipids at the trans-Golgi network resulted in the increased production of IFN-β and other cytokines in THP-1 cells. Furthermore, a mutant STING that could not bind to PI4P failed to traffic from the ER to the Golgi apparatus in response to a STING agonist, whereas forced relocalization of STING to PI4P-enriched areas elicited STING activation in the absence of stimulation with a STING agonist. Thus, PI4P is critical for STING activation, and manipulating PI4P abundance may therapeutically modulate STING-dependent immune responses.
Topics: Phospholipids; Golgi Apparatus; Adaptor Proteins, Signal Transducing
PubMed: 38470955
DOI: 10.1126/scisignal.ade3643 -
Cells Sep 2021Eukaryotic cells contain dynamic membrane-bound organelles that are constantly remodeled in response to physiological and environmental cues. Key organelles are the... (Review)
Review
Eukaryotic cells contain dynamic membrane-bound organelles that are constantly remodeled in response to physiological and environmental cues. Key organelles are the endoplasmic reticulum, the Golgi apparatus and the plasma membrane, which are interconnected by vesicular traffic through the secretory transport route. Numerous viruses, especially enveloped viruses, use and modify compartments of the secretory pathway to promote their replication, assembly and cell egression by hijacking the host cell machinery. In some cases, the subversion mechanism has been uncovered. In this review, we summarize our current understanding of how the secretory pathway is subverted and exploited by viruses belonging to , , and families.
Topics: Biological Transport; Cell Membrane; Endoplasmic Reticulum; Golgi Apparatus; Humans; Secretory Pathway; Viruses
PubMed: 34685515
DOI: 10.3390/cells10102535 -
Cold Spring Harbor Perspectives in... Dec 2011Despite more than six decades of successful Golgi research, the fundamental question as to how biosynthetic material is transported through the secretory pathway remains... (Review)
Review
Despite more than six decades of successful Golgi research, the fundamental question as to how biosynthetic material is transported through the secretory pathway remains unanswered. New technologies such as live cell imaging and correlative microscopy have highlighted the plastic nature of the Golgi, one that is sensitive to perturbation yet highly efficient in regaining both structure and function. Single molecule-microscopy and super resolution-microscopy further adds to this picture. Various models for protein transport have been put forward, each with its own merits and pitfalls but we are far from resolving whether one is more correct than the other. As such, our laboratory considers multiple mechanisms of Golgi transport until proven otherwise. This includes the two classical modes of transport, vesicular transport and cisternal progression/maturation as well as more recent models such as tubular inter- and intra-cisternal connections (long lasting or transient) and inter-Golgi stack transport. In this article, we focus on an emerging inductive technology, mass spectrometry-based proteomics that has already enabled insight into the relative composition of compartments and subcompartments of the secretory pathway including mechanistic aspects of protein transport. We note that proteomics, as with any other technology, is not a stand-alone technology but one that works best alongside complementary approaches.
Topics: Biological Transport; COP-Coated Vesicles; Golgi Apparatus; Proteomics; Vesicular Transport Proteins
PubMed: 21813401
DOI: 10.1101/cshperspect.a005421