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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 -
Seminars in Cell & Developmental Biology Nov 2020In eukaryotic cells, protein sorting is a highly regulated mechanism important for many physiological events. After synthesis in the endoplasmic reticulum and... (Review)
Review
In eukaryotic cells, protein sorting is a highly regulated mechanism important for many physiological events. After synthesis in the endoplasmic reticulum and trafficking to the Golgi apparatus, proteins sort to many different cellular destinations including the endolysosomal system and the extracellular space. Secreted proteins need to be delivered directly to the cell surface. Sorting of secreted proteins from the Golgi apparatus has been a topic of interest for over thirty years, yet there is still no clear understanding of the machinery that forms the post-Golgi carriers. Most evidence points to these post-Golgi carriers being tubular pleomorphic structures that bud from the -face of the Golgi. In this review, we present the background studies and highlight the key components of this pathway, we then discuss the machinery implicated in the formation of these carriers, their translocation across the cytosol, and their fusion at the plasma membrane.
Topics: Animals; Cell Membrane; Golgi Apparatus; Humans; Lipid Metabolism; Membrane Fusion; Protein Transport; Secretory Pathway
PubMed: 32317144
DOI: 10.1016/j.semcdb.2020.04.001 -
ELife Apr 2024Mapping proteins in and associated with the Golgi apparatus reveals how this cellular compartment emerges in budding yeast and progresses over time.
Mapping proteins in and associated with the Golgi apparatus reveals how this cellular compartment emerges in budding yeast and progresses over time.
Topics: Golgi Apparatus; Saccharomycetales
PubMed: 38629949
DOI: 10.7554/eLife.97430 -
Seminars in Cell & Developmental Biology Aug 2018Glycosylation is an important protein modification in all eukaryotes. Whereas the early asparagine-linked glycosylation (N-glycosylation) and N-glycan processing steps... (Review)
Review
Glycosylation is an important protein modification in all eukaryotes. Whereas the early asparagine-linked glycosylation (N-glycosylation) and N-glycan processing steps in the endoplasmic reticulum are conserved between mammals and plants, the maturation of complex N-glycans in the Golgi apparatus differs considerably. Due to a restricted number of Golgi-resident N-glycan processing enzymes and the absence of nucleotide sugars such as CMP-N-acetylneuraminic acid, plants produce only a limited repertoire of different N-glycan structures. Moreover, mammalian mucin-type O-glycosylation of serine or threonine residues has not been described in plants and the required machinery is not encoded in their genome which enables de novo build-up of the pathway. As a consequence, plants are very well-suited for the production of homogenous N- and O-glycans and are increasingly used for the production of recombinant glycoproteins with custom-made glycans that may result in the generation of biopharmaceuticals with improved therapeutic potential.
Topics: Animals; Endoplasmic Reticulum; Glycoproteins; Glycosylation; Golgi Apparatus; Humans; Plants; Protein Processing, Post-Translational
PubMed: 28688929
DOI: 10.1016/j.semcdb.2017.07.005 -
Cell Structure and Function Aug 2019In research on cell biology, organelles have been a major unit of such analyses. Researchers have assumed that the inside of an organelle is almost uniform in regards to... (Review)
Review
In research on cell biology, organelles have been a major unit of such analyses. Researchers have assumed that the inside of an organelle is almost uniform in regards to its function, even though each organelle has multiple functions. However, we are now facing conundrums that cannot be resolved so long as we regard organelles as functionally uniform units. For instance, how can cells control the diverse patterns of glycosylation of various secretory proteins in the endoplasmic reticulum and Golgi in an orderly manner with high accuracy? Here, we introduce the novel concept of organelle zones as a solution; each organelle has functionally distinct zones, and zones in different organelles closely interact each other in order to perform complex cellular functions. This Copernican Revolution from organelle biology to organelle zone biology will drastically change and advance our thoughts about cells.Key words: organelle zone, contact site, ER stress, Golgi stress, organelle autoregulation.
Topics: Animals; Endoplasmic Reticulum; Golgi Apparatus; Humans; Organelles
PubMed: 31308351
DOI: 10.1247/csf.19010 -
Journal of Extracellular Vesicles Nov 2021The extracellular vesicle (EV) surface proteome (surfaceome) acts as a fundamental signalling gateway by bridging intra- and extracellular signalling networks, dictates...
The extracellular vesicle (EV) surface proteome (surfaceome) acts as a fundamental signalling gateway by bridging intra- and extracellular signalling networks, dictates EVs' capacity to communicate and interact with their environment, and is a source of potential disease biomarkers and therapeutic targets. However, our understanding of surface protein composition of large EVs (L-EVs, 100-800 nm, mean 310 nm, ATP5F1A, ATP5F1B, DHX9, GOT2, HSPA5, HSPD1, MDH2, STOML2), a major EV-subtype that are distinct from small EVs (S-EVs, 30-150 nm, mean 110 nm, CD44, CD63, CD81, CD82, CD9, PDCD6IP, SDCBP, TSG101) remains limited. Using a membrane impermeant derivative of biotin to capture surface proteins coupled to mass spectrometry analysis, we show that out of 4143 proteins identified in density-gradient purified L-EVs (1.07-1.11 g/mL, from multiple cancer cell lines), 961 proteins are surface accessible. The surface molecular diversity of L-EVs include (i) bona fide plasma membrane anchored proteins (cluster of differentiation, transporters, receptors and GPI anchored proteins implicated in cell-cell and cell-ECM interactions); and (ii) membrane surface-associated proteins (that are released by divalent ion chelator EDTA) implicated in actin cytoskeleton regulation, junction organization, glycolysis and platelet activation. Ligand-receptor analysis of L-EV surfaceome (e.g., ITGAV/ITGB1) uncovered interactome spanning 172 experimentally verified cognate binding partners (e.g., ANGPTL3, PLG, and VTN) with highest tissue enrichment for liver. Assessment of biotin inaccessible L-EV proteome revealed enrichment for proteins belonging to COPI/II-coated ER/Golgi-derived vesicles and mitochondria. Additionally, despite common surface proteins identified in L-EVs and S-EVs, our data reveals surfaceome heterogeneity between the two EV-subtype. Collectively, our study provides critical insights into diverse proteins operating at the interactive platform of L-EVs and molecular leads for future studies seeking to decipher L-EV heterogeneity and function.
Topics: Cell Line, Tumor; Chromatography, Liquid; Endoplasmic Reticulum; Extracellular Vesicles; Golgi Apparatus; Humans; Membrane Proteins; Mitochondria; Particle Size; Protein Transport; Proteome; Proteomics; Signal Transduction; Tandem Mass Spectrometry
PubMed: 34817906
DOI: 10.1002/jev2.12164 -
Current Opinion in Cell Biology Oct 2022Both neurons and glia in mammalian brains are highly ramified. Neurons form complex neural networks using axons and dendrites. Axons are long with few branches and form... (Review)
Review
Both neurons and glia in mammalian brains are highly ramified. Neurons form complex neural networks using axons and dendrites. Axons are long with few branches and form pre-synaptic boutons that connect to target neurons and effector tissues. Dendrites are shorter, highly branched, and form post-synaptic boutons. Astrocyte processes contact synapses and blood vessels in order to regulate neuronal activity and blood flow, respectively. Oligodendrocyte processes extend toward axons to make myelin sheaths. Microglia processes dynamically survey their environments. Here, we describe the local secretory system (ER and Golgi) in neuronal and glial processes. We focus on Golgi outpost functions in acentrosomal microtubule nucleation, cargo trafficking, and protein glycosylation. Thus, satellite ER and Golgi are critical for local structure and function in neurons and glia.
Topics: Animals; Axons; Dendrites; Golgi Apparatus; Mammals; Neurons; Synapses
PubMed: 35964523
DOI: 10.1016/j.ceb.2022.102119 -
Cells Sep 2020Conventional protein secretion in eukaryotic cells occurs via vesicular trafficking of proteins that are first targeted to the endoplasmic reticulum (ER), through the...
Conventional protein secretion in eukaryotic cells occurs via vesicular trafficking of proteins that are first targeted to the endoplasmic reticulum (ER), through the Golgi apparatus, and subsequently routed to the plasma membrane (PM), where membrane proteins take up residence while luminal proteins are released extracellularly [...].
Topics: Animals; Cell Membrane; Endoplasmic Reticulum; Fungi; Golgi Apparatus; Humans; Membrane Proteins; Plants; Protein Transport
PubMed: 32882862
DOI: 10.3390/cells9092009 -
Current Biology : CB Apr 2018Muschalik and Munro introduce golgins and their roles as vesicle tethers and scaffolds at the Golgi. (Review)
Review
Muschalik and Munro introduce golgins and their roles as vesicle tethers and scaffolds at the Golgi.
Topics: Animals; Autoantigens; Biological Evolution; Evolution, Molecular; Golgi Apparatus; Golgi Matrix Proteins; Humans; Mammals; Membrane Proteins
PubMed: 29689216
DOI: 10.1016/j.cub.2018.01.006 -
ELife Nov 2023A receptor protein called TGN46 has an important role in sorting secretory proteins into vesicles going to different destinations inside cells.
A receptor protein called TGN46 has an important role in sorting secretory proteins into vesicles going to different destinations inside cells.
Topics: trans-Golgi Network; Proteins; Protein Transport; Golgi Apparatus; Secretory Vesicles
PubMed: 37997893
DOI: 10.7554/eLife.93490