Petia Adarska, Luis Wong-Dilworth, Francesca Bottanelli
{"title":"ARF GTPases Function at the Golgi.","authors":"Petia Adarska, Luis Wong-Dilworth, Francesca Bottanelli","doi":"10.1007/978-3-032-16833-7_5","DOIUrl":"10.1007/978-3-032-16833-7_5","url":null,"abstract":"<p><p>ADP-ribosylation factors (ARFs) are small (~21 kDa) GTPases that play a central role in intracellular transport across eukaryotic cells. Structurally related to Ras GTPases, ARFs were initially discovered as allosteric activators of cholera toxin but later emerged as key regulators of membrane trafficking. ARFs function through a GDP-GTP cycle, where guanine nucleotide exchange factors (GEFs) promote the exchange of GDP for GTP, activating ARFs and facilitating their membrane association. Conversely, GTPase-activating proteins (GAPs) stimulate GTP hydrolysis, leading to ARF inactivation and membrane dissociation. This cycle is crucial for ARF-mediated recruitment of cargo adaptors, coat proteins which regulate cargo selection and trafficking pathways through a close interplay with lipid-based signaling.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"93-108"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259494","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Lipid Metabolism and Trafficking in the Golgi Apparatus.","authors":"Jan Parolek, Yeongho Kim, Christopher G Burd","doi":"10.1007/978-3-032-16833-7_8","DOIUrl":"10.1007/978-3-032-16833-7_8","url":null,"abstract":"<p><p>In organelle biogenesis pathways, the Golgi apparatus plays a central role in synthesizing and distributing complex sphingolipids, glycerolipids, and cholesterol, which form the membranes of organelles. The concept of 'lipid flow' describes the circulation of lipids throughout the endomembrane system, mediated by vesicle-based carriers and lipid transfer proteins that directly transfer lipids at sites of organelle-organelle contact. The synthesis and trafficking of lipids are closely interconnected, as they undergo successive enzymatic transformations that begin in the endoplasmic reticulum and are completed in the Golgi apparatus before being distributed to other organelles. A phosphatidylinositol 4-phosphate signaling network that converges on the trans cisterna and trans Golgi network compartments regulates lipid flow to, though, and out of the Golgi apparatus, acting as a rheostat that tunes the rates and specificities of lipid trafficking by controlling phosphatidylinositol 4-phosphate levels in Golgi membranes. The integration of glycolipid and glycoprotein processing reactions within the Golgi with lipid sorting and trafficking pathways suggests that the Golgi apparatus serves as a lipid-based sorting station at the heart of organelle biogenesis pathways.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"177-194"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259575","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Functions of the Golgin Family of Coiled-Coil Proteins.","authors":"Maraym Arab, Martin Lowe","doi":"10.1007/978-3-032-16833-7_4","DOIUrl":"10.1007/978-3-032-16833-7_4","url":null,"abstract":"<p><p>The golgins are a family of ubiquitously expressed and evolutionary conserved Golgi-localised coiled-coil proteins. The golgins are particularly important for vesicle trafficking and structural organisation of the Golgi apparatus. The golgins mediate tethering, or long-range capture, of transport vesicles to Golgi membranes, a key step in vesicle traffic that ensures the specificity of vesicle transport at the Golgi. Following tethering, the golgins associate with other factors to ensure that vesicles undergo the transition to membrane fusion mediated by SNARE proteins. The golgins also contribute to the structural organisation of the Golgi apparatus, particularly in Golgi ribbon formation. This is achieved in several ways, which includes linking the Golgi membranes to the microtubule cytoskeleton, controlling the activity of cytoskeletal regulators and physically linking Golgi elements into the ribbon. Golgin-dependent interactions with the microtubule cytoskeleton also contribute to cell polarity, migration and division. In addition to regulating Golgi function and organisation, the golgins scaffold various factors to control the activity of these factors in a range of cellular processes which includes signaling, autophagy, spindle assembly and cell fate determination. In this book chapter we discuss current understanding of the golgins and their functional roles in cells.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"71-92"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Comparative Study of the Positions of Glycosylated Residues in the Chains of Fibril-Forming Collagens and the Role that These Residues Play in Axial and Lateral Assembly.","authors":"Gillian E Norris, David A D Parry","doi":"10.1007/978-3-032-05273-5_9","DOIUrl":"10.1007/978-3-032-05273-5_9","url":null,"abstract":"<p><p>In this review, we have collected and analysed collagen glycosylation data in an effort to better understand its possible function in fibrillogenesis. Towards that end, we have identified glycosylation sites in many different fibril-forming collagen molecules (Types I, II, III, V, XI and XXIV) and, more importantly, the glycan itself as well as the percentage of collagen molecules in the sample that contain it. As the numbers of quantitative analyses of different collagen types from different species and tissues taken under different physiological conditions grows, a more accurate picture is emerging of the role that collagen O-glycosylation may play in fibrillogenesis. It is becoming increasingly clear that glycosylation does play an important part in the initial stages of the axial assembly of collagen molecules as well as in the lateral control of fibril size. Much remains unknown of the precise mechanisms involved, however, and further detailed analyses will be required before a complete picture of the various in vivo roles played by the glycans emerges.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"255-275"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146012355","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"STING Innate Immunity Signalling from the Golgi.","authors":"Tomohiko Taguchi","doi":"10.1007/978-3-032-16833-7_13","DOIUrl":"10.1007/978-3-032-16833-7_13","url":null,"abstract":"<p><p>The cGAS-STING pathway has recently emerged as a critical driver of inflammation in a variety of settings, such as double-stranded DNA (dsDNA) virus infection, cellular stress, and tissue damage. The pathway senses microbial and host-derived dsDNA in the cytosol, and triggers the production of the type I interferons through the activation of TBK1 (kinase) and IRF3 (transcription factor). The detailed mechanistic understanding of the pathway has enabled the development of pharmacological agents for the treatment of chronic inflammation and cancer. STING is a transmembrane protein that localizes at the endoplasmic reticulum (ER). Once bound to cGAMP, a second messenger that is generated by dsDNA-bound cGAS, STING translocates from the ER to the Golgi. STING then activates TBK1 and IRF3 at the trans-Golgi network (TGN). Dysregulated Golgi-to-ER traffic underlies the pathogenesis of COPA syndrome, a monogenic autoinflammatory disease caused by missense mutations of coatomer protein complex subunit α (COP-α). In this chapter, I focus on emerging issues regarding the regulation of STING activation by membrane traffic between the ER and the Golgi, and also on the molecular mechanism underlying the specific activation of TBK1/IRF3 at the TGN.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"317-329"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Dalia O Saleh, Mohamed L Salem, Sophie Van Linthout, Queran Lin, Nadia M Hamdy
{"title":"Epigenetic Modulation of Immunity: Mechanisms, Implications, and Emerging Therapeutic Horizons; a Step Toward Epigenetics to Precision.","authors":"Dalia O Saleh, Mohamed L Salem, Sophie Van Linthout, Queran Lin, Nadia M Hamdy","doi":"10.1007/978-3-032-08530-6_1","DOIUrl":"10.1007/978-3-032-08530-6_1","url":null,"abstract":"<p><p>Epigenetic regulation plays a central role in immune cell development, specialization, and memory formation by dynamically modifying DNA, histones, and RNA. These processes enable adaptation to environmental cues, precise pathogen responses, and maintenance of immune tolerance, while their disruption contributes to autoimmune, inflammatory, and cancer pathogenesis. DNA methylation, histone modifications, and noncoding RNA regulation shape the lineage and activation states of T cells, B cells, macrophages, and natural killer (NK) cells, with specific alterations linked to diseases, such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Emerging insights also highlight roles for RNA modifications and exosome-mediated RNA transfer in immune activation, trained immunity, and antigen presentation. Advances in single-cell epigenomics, CRISPR-based editing, and RNA sequencing are driving the development of targeted therapies-such as DNA methyltransferase (DNMT) inhibitors, histone deacetylase (HDAC) inhibitors, RNA-based interventions, and exosome delivery systems-that aim to reprogram immune responses. Understanding immune cell epigenetics paves the way for precision immunotherapies tailored to patient-specific profiles, offering highly specific, effective treatments with minimal immune suppression.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"1-59"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cisternal Maturation of the Golgi Apparatus in Budding Yeast.","authors":"Takuro Tojima, Akihiko Nakano","doi":"10.1007/978-3-032-06936-8_12","DOIUrl":"10.1007/978-3-032-06936-8_12","url":null,"abstract":"<p><p>The Golgi apparatus in the budding yeast Saccharomyces cerevisiae, unlike those in mammalian and plant cells, does not form stacks but exists as multiple separate cisternae scattered throughout the cytoplasm. This unique morphological feature has allowed us to observe the spatiotemporal dynamics of individual Golgi cisternae by live cell imaging. Nearly two decades ago, we developed super-resolution confocal live imaging microscopy (SCLIM) and visualized that the yeast Golgi truly matures, i.e., a single cisterna gradually changes its nature from cis to trans cisternae over time. Since then to date, many researchers have observed a wide variety of proteins residing in and around the Golgi, as well as cargoes, in live yeast cells, unveiling the detailed step-by-step processes of Golgi cisternal maturation. Notably, our recent studies identified the ER-Golgi intermediate compartment (ERGIC) in budding yeast, which matures into the cis Golgi. After cis-to-trans maturation, the trans Golgi further matures into the trans-Golgi network (TGN), which can be divided into at least two sub-stages, the early and late TGN. Altogether, accumulating evidence revealed that the Golgi apparatus is not a static, but rather a highly dynamic organelle that appears transiently with a short lifetime along with cargo traffic.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"287-311"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522845","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cargo Sorting Zones in Plant Trans-Golgi Network.","authors":"Yutaro Shimizu, Tomohiro Uemura","doi":"10.1007/978-3-032-16833-7_9","DOIUrl":"10.1007/978-3-032-16833-7_9","url":null,"abstract":"<p><p>Membrane trafficking is crucial for various aspects of plant growth, development, and responses to environmental stimuli. The trans-Golgi network (TGN) in plants serves as a central sorting station for membrane trafficking and operates at the intersection of the biosynthetic and endocytic pathways for both plasma membrane/extracellular molecules and vacuolar proteins. Although the molecular machinery that controls membrane trafficking is evolutionarily conserved, how plant TGNs perform their multiple sorting operations still remains poorly understood. Multitasking of plant TGNs manifests as a partition of the molecular machinery within a single organelle. This chapter presents the current state of knowledge on plant TGNs, explores emerging concepts in the field, and highlights key questions and challenges for future research.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"195-217"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion.","authors":"Meir Aridor","doi":"10.1007/978-3-032-16833-7_1","DOIUrl":"10.1007/978-3-032-16833-7_1","url":null,"abstract":"<p><p>Biosynthetic secretion mobilizes about a third of the human proteome from the Endoplasmic Reticulum (ER) in route to cellular and extracellular destinations. Traffic from the ER to the Golgi Complex begins at distinct sites on the ER, the ER exit sites (ERES), which are functionally and physically connected with the Golgi. ERES are the first sorting sites in the secretory pathway. This chapter explores key molecular functionalities of the ERES.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"3-36"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Biomolecular Condensates in and Around the ER-Golgi Interface.","authors":"Miguel Ruiz, Savannah M Bogus, Andreas M Ernst","doi":"10.1007/978-3-032-06936-8_9","DOIUrl":"10.1007/978-3-032-06936-8_9","url":null,"abstract":"<p><p>Biomolecular condensates represent a new paradigm of cytoplasmic organization. In recent years, an increasing amount of evidence suggests that protein condensates can directly impact the morphology and function of membrane compartments. The early secretory pathway, which comprises the ER and Golgi compartments, is emerging as a hotspot for biomolecular condensates. In this chapter, we discuss recent reports suggesting diverse roles for condensates in cargo sorting, regulating membrane traffic, and shaping organelle morphology. This promotes a view in which biomolecular condensates may significantly contribute to defining the anatomy and specific functions of the Golgi and its surrounding membranes.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"221-243"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}