Advances in biological regulation最新文献

{"title":"Sixty-fourth international symposium on biological regulation and enzyme activity in normal and neoplastic tissues","authors":"","doi":"10.1016/j.jbior.2024.101017","DOIUrl":"10.1016/j.jbior.2024.101017","url":null,"abstract":"","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101017"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2212492624000058/pdfft?md5=c4ff8cf58a997a4bdc75268d6cd3c270&pid=1-s2.0-S2212492624000058-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139511556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role and regulation of phospholipase D in metabolic disorders","authors":"Seon Hyang Park ,&nbsp;Ji Hyeon Kang ,&nbsp;Yoe-Sik Bae","doi":"10.1016/j.jbior.2023.100988","DOIUrl":"10.1016/j.jbior.2023.100988","url":null,"abstract":"<div><p>Phospholipase D (PLD) is an enzyme that catalyzes the hydrolysis of phosphatidylcholine into phosphatidic acid and free choline. In mammals, PLD exists in two well-characterized isoforms, PLD1 and PLD2, and it plays pivotal roles as signaling mediators in various cellular functions, such as cell survival, differentiation, and migration. These isoforms are predominantly expressed in diverse cell types, including many immune cells, such as monocytes and macrophages, as well as non-immune cells, such as epithelial and endothelial cells. Several previous studies have revealed that the stimulation of these cells leads to an increase in PLD expression and its enzymatic products, potentially influencing the pathological responses in a wide spectrum of diseases. Metabolic diseases, exemplified by conditions, such as diabetes, obesity, hypertension, and atherosclerosis, pose significant global health challenges. Abnormal activation or dysfunction of PLD emerges as a potential contributing factor to the pathogenesis and progression of these metabolic disorders. Therefore, it is crucial to thoroughly investigate and understand the intricate relationship between PLD and metabolic diseases. In this review, we provide an in-depth overview of the functional roles and molecular mechanisms of PLD involved in metabolic diseases. By delving into the intricate interplay between PLD and metabolic disorders, this review aims to offer insights into the potential therapeutic interventions.</p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 100988"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41231575","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":"Flimsy overlay","authors":"Lucio Ildebrando cocco","doi":"10.1016/j.jbior.2024.101019","DOIUrl":"10.1016/j.jbior.2024.101019","url":null,"abstract":"","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101019"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2212492624000071/pdfft?md5=4eb588ae2be05b36d65071eb8f2f3c19&pid=1-s2.0-S2212492624000071-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139502125","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Three kingdoms and one ceramide to rule them all. A comparison of the structural basis of ceramide-dependent regulation of sphingolipid biosynthesis in animals, plants, and fungi","authors":"Mohammed H. AL Mughram ,&nbsp;Glen E. Kellogg ,&nbsp;Binks W. Wattenberg","doi":"10.1016/j.jbior.2023.101010","DOIUrl":"10.1016/j.jbior.2023.101010","url":null,"abstract":"<div><p>Sphingolipids are a diverse class of lipids with essential functions as determinants of membrane physical properties and as intra- and intercellular signaling agents. Disruption of the normal biochemical processes that establish the levels of individual sphingolipids is associated with a variety of human diseases including cancer, cardiovascular disease, metabolic disease, skin diseases, and lysosomal storage diseases. A unique aspect of this metabolic network is that there is a single enzymatic step that initiates the biosynthetic pathway for all sphingolipids. This step is catalyzed by the enzyme serine palmitoyltranserase (SPT). Under most circumstances SPT condenses serine and the 16-carbon acyl-CoA, palmitoyl-CoA to produce the precursor of all sphingolipids. SPT, a four-subunit protein complex, is subject to classic feedback regulation: when cellular sphingolipids are elevated, SPT activity is inhibited. Ceramide is the sphingolipid sensed by this system and it regulates SPT by directly binding to the complex. The ceramide binding site in the SPT complex, and how ceramide binding results in SPT inhibition, has now been determined in vertebrates, plants, and yeast using molecular modeling and cryo-electron microscopy. Here we discuss the similarities and differences revealed by these resolved structures and the surprising result that ceramide binds at almost identical positions in the SPT complex of these divergent organisms, but accomplishes SPT regulation in very different ways.</p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101010"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138883866","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":"A new role for phosphoinositides in regulating mitochondrial dynamics","authors":"Sonia Raveena Lourdes ,&nbsp;Rajendra Gurung ,&nbsp;Saveen Giri ,&nbsp;Christina A. Mitchell ,&nbsp;Meagan J. McGrath","doi":"10.1016/j.jbior.2023.101001","DOIUrl":"10.1016/j.jbior.2023.101001","url":null,"abstract":"<div><p>Phosphoinositides are a minor group of membrane-associated phospholipids that are transiently generated on the cytoplasmic leaflet of many organelle membranes and the plasma membrane. There are seven functionally distinct phosphoinositides, each derived via the reversible phosphorylation of phosphatidylinositol in various combinations on the inositol ring. Their generation and termination is tightly regulated by phosphatidylinositol-kinases and –phosphatases. These enzymes can function together in an integrated and coordinated manner, whereby the phosphoinositide product of one enzyme may subsequently serve as a substrate for another to generate a different phosphoinositide species. This regulatory mechanism not only enables the transient generation of phosphoinositides on membranes, but also more complex sequential or bidirectional conversion pathways, and phosphoinositides can also be transferred between organelles via membrane contacts. It is this capacity to fine-tune phosphoinositide signals that makes them ideal regulators of membrane organization and dynamics, through their recruitment of signalling, membrane altering and lipid transfer proteins. Research spanning several decades has provided extensive evidence that phosphoinositides are major gatekeepers of membrane organization, with roles in endocytosis, exocytosis, autophagy, lysosome dynamics, vesicular transport and secretion, cilia, inter-organelle membrane contact, endosome maturation and nuclear function. By contrast, there has been remarkably little known about the role of phosphoinositides at mitochondria – an enigmatic and major knowledge gap, with challenges in reliably detecting phosphoinositides at this site.</p><p>Here we review recent significant breakthroughs in understanding the role of phosphoinositides in regulating mitochondrial dynamics and metabolic function.</p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101001"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2212492623000477/pdfft?md5=213ae24683ebcf7cf751280c561481ab&pid=1-s2.0-S2212492623000477-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138497534","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Coordinated inositide lipid-phosphatase activities of synaptojanin modulates actin cytoskeleton organization","authors":"Tong Zhang ,&nbsp;Andrew T. Hale ,&nbsp;Shuling Guo ,&nbsp;John D. York","doi":"10.1016/j.jbior.2023.101012","DOIUrl":"10.1016/j.jbior.2023.101012","url":null,"abstract":"<div><p>Synaptojanin proteins are evolutionarily conserved regulators of vesicle transport and membrane homeostasis. Disruption of synaptojanin function has been implicated in a wide range of neurological disorders. Synaptojanins act as dual-functional lipid phosphatases capable of hydrolyzing a variety of phosphoinositides (PIPs) through autonomous <em>SAC1</em>-like PIP 4-phosphatase and PIP₂ 5-phosphatase domains. The rarity of an evolutionary configuration of tethering two distinct enzyme activities in a single protein prompted us to investigate their individual and combined roles in budding yeast. Both PIP and PIP₂ phosphatase activities are encoded by multiple gene products and are independently essential for cell viability. In contrast, we observed that the synaptojanin proteins utilized both lipid-phosphatase activities to properly coordinate polarized distribution of actin during the cell cycle. Expression of each activity untethered (<em>in trans</em>) failed to properly reconstitute the basal actin regulatory activity; whereas tethering (<em>in cis</em>), even through synthetic linkers, was sufficient to complement these defects. Studies of chimeric proteins harboring PIP and PIP₂ phosphatase domains from a variety of gene products indicate synaptojanin proteins have highly specialized activities and that the length of the linker between the lipid-phosphatase domains is critical for actin regulatory activity. Our data are consistent with synaptojanin possessing a strict requirement for both two-domain configuration for some but not all functions and provide mechanistic insights into a coordinated role of tethering distinct lipid-phosphatase activities.</p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101012"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2212492623000581/pdfft?md5=9765a94c0e2c924c2b070427e61ef1c8&pid=1-s2.0-S2212492623000581-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139456404","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deciphering signaling pathways in hematopoietic stem cells: the molecular complexity of Myelodysplastic Syndromes (MDS) and leukemic progression","authors":"Irene Casalin ,&nbsp;Alessia De Stefano ,&nbsp;Eleonora Ceneri ,&nbsp;Alessandra Cappellini ,&nbsp;Carlo Finelli ,&nbsp;Antonio Curti ,&nbsp;Stefania Paolini ,&nbsp;Sarah Parisi ,&nbsp;Letizia Zannoni ,&nbsp;Jacqueline Boultwood ,&nbsp;James A. McCubrey ,&nbsp;Pann-Ghill Suh ,&nbsp;Giulia Ramazzotti ,&nbsp;Roberta Fiume ,&nbsp;Stefano Ratti ,&nbsp;Lucia Manzoli ,&nbsp;Lucio Cocco ,&nbsp;Matilde Y. Follo","doi":"10.1016/j.jbior.2024.101014","DOIUrl":"10.1016/j.jbior.2024.101014","url":null,"abstract":"<div><p>Myelodysplastic Syndromes, a heterogeneous group of hematological disorders, are characterized by abnormalities in phosphoinositide-dependent signaling, epigenetic regulators, apoptosis, and cytokine interactions within the bone marrow microenvironment, contributing to disease pathogenesis and neoplastic growth. Comprehensive knowledge of these pathways is crucial for the development of innovative therapies that aim to restore normal apoptosis and improve patient outcomes.</p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101014"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2212492624000022/pdfft?md5=14abee68b88a77ad36e9857499a566e7&pid=1-s2.0-S2212492624000022-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139502123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biological function, topology, and quantification of plasma membrane Ceramide","authors":"Daniel Canals ,&nbsp;Yusuf A. Hannun","doi":"10.1016/j.jbior.2023.101009","DOIUrl":"10.1016/j.jbior.2023.101009","url":null,"abstract":"<div><p><span>Over the past 30 years, a growing body of evidence has revealed the regulatory role of the lipid </span>ceramide<span> in various cellular functions. The structural diversity of ceramide, resulting in numerous species, and its distinct distribution within subcellular compartments may account for its wide range of functions. However, our ability to study the potential role of ceramide in specific subcellular membranes has been limited. Several works have shown mitochondrial, Golgi, and plasma membrane ceramide to mediate signaling pathways<span> independently. These results have started to shift the focus on ceramide signaling research toward specific membrane pools. Nonetheless, the challenge arises from the substantial intracellular ceramide content, hindering efforts to quantify its presence in particular membranes. Recently, we have developed the first method capable of detecting and quantifying ceramide in the plasma membrane, leading to unexpected results such as detecting different pools of ceramide responding to drug concentration or time. This review summarizes the historical context that defined the idea of pools of ceramide, the studies on plasma membrane ceramide as a bioactive entity, and the tools available for its study, especially the new method to detect and, for the first time, quantify plasma membrane ceramide. We believe this method will open new avenues for researching sphingolipid signaling and metabolism.</span></span></p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101009"},"PeriodicalIF":0.0,"publicationDate":"2023-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138827589","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":"Mechanistic insight on the role of iRhom2-TNF-α-BAFF signaling pathway in various autoimmune disorders","authors":"Shradha Devi Dwivedi ,&nbsp;Rashi Shukla ,&nbsp;Krishna Yadav ,&nbsp;Lokendra Singh Rathor ,&nbsp;Deependra Singh ,&nbsp;Manju Rawat Singh","doi":"10.1016/j.jbior.2023.101011","DOIUrl":"10.1016/j.jbior.2023.101011","url":null,"abstract":"<div><p><span><span><span>iRhom2 is a crucial cofactor involved in upregulation of TNF receptors<span> (TNFRs) and the pro-inflammatory cytokine tumor necrosis factor (TNF-) from the cell surface by </span></span>ADAM17. Tumor necrosis factor- α converting </span>enzyme<span><span> (TACE) is another name given to ADAM17. Many membrane attached biologically active molecules are cleaved by this enzyme which includes TNFRs<span><span> and the pro-inflammatory cytokine tumor necrosis factor- α. The TNF receptors are of two types TNFR1 and TNFR2. iRhom2 belongs to the pseudo-protease class of rhomboid family, its abundance is observed in the immune cells. </span>Biological activity of ADAM17 is affected in multiple levels by the iRhom2. ADAM17 is trafficked into the </span></span>Golgi apparatus by the action of iRhom2, where it gets matured proteolytically and is stimulated to perform its function on the cell surface. This process of activation of ADAM17 results in the protection of the organism from the cascade of inflammatory reactions, as this activation blocks the TNF- α mediated secretion responsible for inflammatory responses produced. Present paper illustrates about the iRhom2-TNF-α-BAFF </span></span>signaling pathway<span> and its correlation with several autoimmune disorders such as Rheumatoid Arthritis, Systemic Lupus Erythematosus, Hemophilia Arthropathy, Alzheimer's disease and Tylosis with esophageal cancer etc.</span></p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"92 ","pages":"Article 101011"},"PeriodicalIF":0.0,"publicationDate":"2023-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139020958","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":"IP8: A quantitatively minor inositol pyrophosphate signaling molecule that punches above its weight","authors":"Chunfang Gu ,&nbsp;Xingyao Li ,&nbsp;Guangning Zong ,&nbsp;Huanchen Wang ,&nbsp;Stephen B. Shears","doi":"10.1016/j.jbior.2023.101002","DOIUrl":"https://doi.org/10.1016/j.jbior.2023.101002","url":null,"abstract":"<div><p><span>The inositol<span> pyrophosphates (PP-IPs) are specialized members of the wider inositol phosphate signaling family that possess functionally significant diphosphate groups. The PP-IPs exhibit remarkable functionally versatility throughout the eukaryotic kingdoms. However, a quantitatively minor PP-IP – 1,5 bisdiphosphoinositol tetrakisphosphate (1,5-IP</span></span>₈<span>) – has received considerably less attention from the cell signalling community. The main purpose of this review is to summarize recently-published data which have now brought 1,5-IP</span>₈<span> into the spotlight, by expanding insight into the molecular mechanisms by which this polyphosphate regulates many fundamental biological processes.</span></p></div>","PeriodicalId":7214,"journal":{"name":"Advances in biological regulation","volume":"91 ","pages":"Article 101002"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138557336","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}