TrafficPub Date : 2022-05-23DOI: 10.1111/tra.12859
Pravin Hivare, Joshna Gadhavi, D. Bhatia, Sharad Gupta
{"title":"α‐Synuclein fibrils explore actin‐mediated macropinocytosis for cellular entry into model neuroblastoma neurons","authors":"Pravin Hivare, Joshna Gadhavi, D. Bhatia, Sharad Gupta","doi":"10.1111/tra.12859","DOIUrl":"https://doi.org/10.1111/tra.12859","url":null,"abstract":"Alpha‐synuclein (α‐Syn), an intrinsically disordered protein (IDP), is associated with neurodegenerative disorders, including Parkinson's disease (PD or other α‐synucleinopathies. Recent investigations propose the transmission of α‐Syn protein fibrils, in a prion‐like manner, by entering proximal cells to seed further fibrillization in PD. Despite the recent advances, the mechanisms by which extracellular protein aggregates internalize into the cells remain poorly understood. Using a simple cell‐based model of human neuroblastoma‐derived differentiated neurons, we present the cellular internalization of α‐Syn PFF to check cellular uptake and recycling kinetics along with the standard endocytic markers Transferrin (Tf) marking clathrin‐mediated endocytosis (CME) and Galectin3 (Gal3) marking clathrin‐independent endocytosis (CIE). Specific inhibition of endocytic pathways using chemical inhibitors reveals no significant involvement of CME, CIE and caveolae‐mediated endocytosis (CvME). A substantial reduction in cellular uptake was observed after perturbation of actin polymerization and treatment with macropinosomes inhibitor. Our results show that α‐Syn PFF mainly internalizes into the SH‐SY5Y cells and differentiated neurons via the macropinocytosis pathway. The elucidation of the molecular and cellular mechanism involved in the α‐Syn PFF internalization will help improve the understanding of α‐synucleinopathies including PD, and further design specific inhibitors for the same.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89127590","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-05-16DOI: 10.1111/tra.12846
Dajana Tanasic, N. Berns, V. Riechmann
{"title":"Myosin V facilitates polarised E‐cadherin secretion","authors":"Dajana Tanasic, N. Berns, V. Riechmann","doi":"10.1111/tra.12846","DOIUrl":"https://doi.org/10.1111/tra.12846","url":null,"abstract":"E‐cadherin has a fundamental role in epithelial tissues by providing cell–cell adhesion. Polarised E‐cadherin exocytosis to the lateral plasma membrane is central for cell polarity and epithelial homeostasis. Loss of E‐cadherin secretion compromises tissue integrity and is a prerequisite for metastasis. Despite this pivotal role of E‐cadherin secretion, the transport mechanism is still unknown. Here we identify Myosin V as the motor for E‐cadherin secretion. Our data reveal that Myosin V and F‐actin are required for the formation of a continuous apicolateral E‐cadherin belt, the zonula adherens. We show by live imaging how Myosin V transports E‐cadherin vesicles to the plasma membrane, and distinguish two distinct transport tracks: an apical actin network leading to the zonula adherens and parallel actin bundles leading to the basal‐most region of the lateral membrane. E‐cadherin secretion starts in endosomes, where Rab11 and Sec15 recruit Myosin V for transport to the zonula adherens. We also shed light on the endosomal sorting of E‐cadherin by showing how Rab7 and Snx16 cooperate in moving E‐cadherin into the Rab11 compartment. Thus, our data help to understand how polarised E‐cadherin secretion maintains epithelial architecture and prevents metastasis.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90245460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-05-01Epub Date: 2022-04-24DOI: 10.1111/tra.12839
Duarte C Barral, Leopoldo Staiano, Cláudia Guimas Almeida, Dan F Cutler, Emily R Eden, Clare E Futter, Antony Galione, André R A Marques, Diego Luis Medina, Gennaro Napolitano, Carmine Settembre, Otília V Vieira, Johannes M F G Aerts, Peace Atakpa-Adaji, Gemma Bruno, Antonella Capuozzo, Elvira De Leonibus, Chiara Di Malta, Cristina Escrevente, Alessandra Esposito, Paolo Grumati, Michael J Hall, Rita O Teodoro, Susana S Lopes, J Paul Luzio, Jlenia Monfregola, Sandro Montefusco, Frances M Platt, Roman Polishchuck, Maria De Risi, Irene Sambri, Chiara Soldati, Miguel C Seabra
{"title":"Current methods to analyze lysosome morphology, positioning, motility and function.","authors":"Duarte C Barral, Leopoldo Staiano, Cláudia Guimas Almeida, Dan F Cutler, Emily R Eden, Clare E Futter, Antony Galione, André R A Marques, Diego Luis Medina, Gennaro Napolitano, Carmine Settembre, Otília V Vieira, Johannes M F G Aerts, Peace Atakpa-Adaji, Gemma Bruno, Antonella Capuozzo, Elvira De Leonibus, Chiara Di Malta, Cristina Escrevente, Alessandra Esposito, Paolo Grumati, Michael J Hall, Rita O Teodoro, Susana S Lopes, J Paul Luzio, Jlenia Monfregola, Sandro Montefusco, Frances M Platt, Roman Polishchuck, Maria De Risi, Irene Sambri, Chiara Soldati, Miguel C Seabra","doi":"10.1111/tra.12839","DOIUrl":"10.1111/tra.12839","url":null,"abstract":"<p><p>Since the discovery of lysosomes more than 70 years ago, much has been learned about the functions of these organelles. Lysosomes were regarded as exclusively degradative organelles, but more recent research has shown that they play essential roles in several other cellular functions, such as nutrient sensing, intracellular signalling and metabolism. Methodological advances played a key part in generating our current knowledge about the biology of this multifaceted organelle. In this review, we cover current methods used to analyze lysosome morphology, positioning, motility and function. We highlight the principles behind these methods, the methodological strategies and their advantages and limitations. To extract accurate information and avoid misinterpretations, we discuss the best strategies to identify lysosomes and assess their characteristics and functions. With this review, we aim to stimulate an increase in the quantity and quality of research on lysosomes and further ground-breaking discoveries on an organelle that continues to surprise and excite cell biologists.</p>","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9323414/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10857319","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-04-24DOI: 10.1111/tra.12840
A. Bonhoure, L. Henry, C. Bich, L. Blanc, Blanche Bergeret, M. Bousquet, O. Coux, P. Stoebner, M. Vidal
{"title":"Extracellular 20S proteasome secreted via microvesicles can degrade poorly folded proteins and inhibit Galectin‐3 agglutination activity","authors":"A. Bonhoure, L. Henry, C. Bich, L. Blanc, Blanche Bergeret, M. Bousquet, O. Coux, P. Stoebner, M. Vidal","doi":"10.1111/tra.12840","DOIUrl":"https://doi.org/10.1111/tra.12840","url":null,"abstract":"Proteasomes are major non‐lysosomal proteolytic complexes localized in the cytoplasm and in the nucleus of eukaryotic cells. Strikingly, high levels of extracellular proteasome have also been evidenced in the plasma (p‐proteasome) of patients with specific diseases. Here, we examined the process by which proteasomes are secreted, as well as their structural and functional features once in the extracellular space. We demonstrate that assembled 20S core particles are secreted by cells within microvesicles budding from the plasma membrane. Part of the extracellular proteasome pool is also free of membranes in the supernatant of cultured cells, and likely originates from microvesicles leakage. We further demonstrate that this free proteasome released by cells (cc‐proteasome for cell culture proteasome) possesses latent proteolytic activity and can degrade various extracellular proteins. Both standard (no immune‐subunits) and intermediate (containing some immune‐subunits) forms of 20S are observed. Moreover, we show that galectin‐3, which displays a highly disordered N‐terminal region, is efficiently cleaved by purified cc‐proteasome, without SDS activation, likely after its binding to PSMA3 (α7) subunit through its intrinsically disordered region. As a consequence, galectin‐3 is unable to induce red blood cells agglutination when preincubated with cc‐proteasome. These results highlight potential novel physio‐ and pathologic functions for the extracellular proteasome.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73191740","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-04-22DOI: 10.1111/tra.12844
Tiantian Qian, Chenlu Li, Furong Liu, K. Xu, Chun Wan, Yinghui Liu, Haijia Yu
{"title":"Arabidopsis synaptotagmin 1 mediates lipid transport in a lipid composition‐dependent manner","authors":"Tiantian Qian, Chenlu Li, Furong Liu, K. Xu, Chun Wan, Yinghui Liu, Haijia Yu","doi":"10.1111/tra.12844","DOIUrl":"https://doi.org/10.1111/tra.12844","url":null,"abstract":"The endoplasmic reticulum (ER)‐plasma membrane (PM) contact sites (EPCSs) are structurally conserved in eukaryotes. The Arabidopsis ER‐anchored synaptotagmin 1 (SYT1), enriched in EPCSs, plays a critical role in plant abiotic stress tolerance. It has become clear that SYT1 interacts with PM to mediate ER‐PM connectivity. However, whether SYT1 performs additional functions at EPCSs remains unknown. Here, we report that SYT1 efficiently transfers phospholipids between membranes. The lipid transfer activity of SYT1 is highly dependent on phosphatidylinositol 4,5‐bisphosphate [PI(4,5)P2], a signal lipid accumulated at the PM under abiotic stress. Mechanically, while SYT1 transfers lipids fundamentally through the synaptotagmin‐like mitochondrial‐lipid‐binding protein (SMP) domain, the efficient lipid transport requires the C2A domain‐mediated membrane tethering. Interestingly, we observed that Ca2+ could stimulate SYT1‐mediated lipid transport. In addition to PI(4,5)P2, the Ca2+ activation requires the phosphatidylserine, another negatively charged lipid on the opposed membrane. Together, our studies identified Arabidopsis SYT1 as a lipid transfer protein at EPCSs and demonstrated that it takes conserved as well as divergent mechanisms with other extend‐synaptotagmins. The critical role of lipid composition and Ca2+ reveals that SYT1‐mediated lipid transport is highly regulated by signals in response to abiotic stresses.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90737497","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-04-12DOI: 10.1111/tra.12842
A. Ciesielska, Marta Krawczy, H. Sas-Nowosielska, A. Hromada-Judycka, K. Kwiatkowska
{"title":"CD14 recycling modulates LPS‐induced inflammatory responses of murine macrophages","authors":"A. Ciesielska, Marta Krawczy, H. Sas-Nowosielska, A. Hromada-Judycka, K. Kwiatkowska","doi":"10.1111/tra.12842","DOIUrl":"https://doi.org/10.1111/tra.12842","url":null,"abstract":"TLR4 is activated by the bacterial endotoxin lipopolysaccharide (LPS) and triggers two proinflammatory signaling cascades: a MyD88‐dependent one in the plasma membrane, and the following TRIF‐dependent one in endosomes. An inadequate inflammatory reaction can be detrimental for the organism by leading to sepsis. Therefore, novel approaches to therapeutic modulation of TLR4 signaling are being sought after. The TLR4 activity is tightly connected with the presence of CD14, a GPI‐anchored protein that transfers LPS monomers to the receptor and controls its endocytosis. In this study we focused on CD14 trafficking as a still poorly understood factor affecting TLR4 activity. Two independent assays were used to show that after endocytosis CD14 can recycle back to the plasma membrane in both unstimulated and stimulated cells. This route of CD14 trafficking can be controlled by sorting nexins (SNX) 1, 2 and 6, and is important for maintaining the surface level and the total level of CD14, but can also affect the amount of TLR4. Silencing of these SNXs attenuated especially the CD14‐dependent endosomal signaling of TLR4, making them a new target for therapeutic regulation of the inflammatory response of macrophages to LPS.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80666875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-04-01Epub Date: 2022-03-01DOI: 10.1111/tra.12834
Elisabeth Richardson, Joel B Dacks
{"title":"Distribution of membrane trafficking system components across ciliate diversity highlights heterogenous organelle-associated machinery.","authors":"Elisabeth Richardson, Joel B Dacks","doi":"10.1111/tra.12834","DOIUrl":"https://doi.org/10.1111/tra.12834","url":null,"abstract":"<p><p>The ciliate phylum is a group of protists noted for their unusual membrane trafficking system and apparent environmental ubiquity; as highly successful microbial predators, they are found in all manner of environments and the ability for specific species to adapt to extremely challenging conditions makes them valued as bioindicators. Ciliates have also been used for many years as cell biological models because of their large cell size and ease of culturing, and for many fundamental cell structures, particularly membrane-bound organelles, ciliates were some of the earliest organisms in which these were observed via microscopy. In this study, we carried out a comparative genomic survey of selected membrane trafficking proteins in a pan-ciliate transcriptome and genome dataset. We observed considerable loss of membrane trafficking system (MTS) proteins that would indicate a loss of machinery that is generally conserved across eukaryotic diversity, even after controlling for potentially incomplete genome representation. In particular, the complete DSL1 complex was missing in all surveyed ciliates. This protein complex has been shown as involved in peroxisome biogenesis in some model systems, and a paucity of DSL1 components has been indicative of degenerate peroxisome. However, Tetrahymena thermophila (formerly Tetrahymena pyroformis) was one of the original models for visualizing peroxisomes. Conversely, the AP3 complex essential for mucocyst maturation in T. thermophila, is poorly conserved despite the presence of secretory lysosome-related organelles across ciliate diversity. We discuss potential resolutions for these apparent paradoxes in the context of the heterogenous distribution of MTS machinery across the diversity of ciliates.</p>","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39895916","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-04-01Epub Date: 2022-02-21DOI: 10.1111/tra.12836
Maya Cabot, Volker Kiessling, Judith M White, Lukas K Tamm
{"title":"Endosomes supporting fusion mediated by vesicular stomatitis virus glycoprotein have distinctive motion and acidification.","authors":"Maya Cabot, Volker Kiessling, Judith M White, Lukas K Tamm","doi":"10.1111/tra.12836","DOIUrl":"10.1111/tra.12836","url":null,"abstract":"<p><p>Most enveloped viruses infect cells by binding receptors at the cell surface and undergo trafficking through the endocytic pathway to a compartment with the requisite conditions to trigger fusion with a host endosomal membrane. Broad categories of compartments in the endocytic pathway include early and late endosomes, which can be further categorized into subpopulations with differing rates of maturation and motility characteristics. Endocytic compartments have varying protein and lipid components, luminal ionic conditions and pH that provide uniquely hospitable environments for specific viruses to fuse. In order to characterize compartments that permit fusion, we studied the trafficking and fusion of viral particles pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G) on their surface and equipped with a novel pH sensor and a fluorescent content marker to measure pH, motion and fusion at the single particle level in live cells. We found that the VSV-G particles fuse predominantly from more acidic and more motile endosomes, and that a significant fraction of particles is trafficked to more static and less acidic endosomes that do not support their fusion. Moreover, the fusion-supporting endosomes undergo directed motion.</p>","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10621750/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39909085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-03-08DOI: 10.1111/tra.12838
S. Barmaver, Muniesh Muthaiyan Shanmugam, Yen Chang, Odvogmed Bayansan, Prerana Bhan, Gong-Her Wu, O. I. Wagner
{"title":"Loss of intermediate filament IFB‐1 reduces mobility, density, and physiological function of mitochondria in Caenorhabditis elegans sensory neurons","authors":"S. Barmaver, Muniesh Muthaiyan Shanmugam, Yen Chang, Odvogmed Bayansan, Prerana Bhan, Gong-Her Wu, O. I. Wagner","doi":"10.1111/tra.12838","DOIUrl":"https://doi.org/10.1111/tra.12838","url":null,"abstract":"Mitochondria and intermediate filament (IF) accumulations often occur during imbalanced axonal transport leading to various types of neurological diseases. It is still poorly understood whether a link between neuronal IFs and mitochondrial mobility exist. In Caenorhabditis elegans, among the 11 cytoplasmic IF family proteins, IFB‐1 is of particular interest as it is expressed in a subset of sensory neurons. Depletion of IFB‐1 leads to mild dye‐filling and significant chemotaxis defects as well as reduced life span. Sensory neuron development is affected and mitochondrial transport is slowed down leading to reduced densities of these organelles. Mitochondria tend to cluster in neurons of IFB‐1 mutants likely independent of the fission and fusion machinery. Oxygen consumption and mitochondrial membrane potential is measurably reduced in worms carrying mutations in the ifb‐1 gene. Membrane potential also seems to play a role in transport such as carbonyl cyanide p‐(trifluoromethoxy)phenylhydrazone treatment led to increased directional switching of mitochondria. Mitochondria co‐localize with IFB‐1 in worm neurons and appear in a complex with IFB‐1 in pull‐down assays. In summary, we propose a model in which neuronal IFs may serve as critical (transient) anchor points for mitochondria during their long‐range transport in neurons for steady and balanced transport.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72945105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
TrafficPub Date : 2022-03-01Epub Date: 2022-02-02DOI: 10.1111/tra.12832
María de Los Ángeles Juricic Urzúa, Javiera Gallardo Rojas, Andrés Couve Correa, Mauricio Cerda, Steffen Härtel Gründler, Carolina González-Silva
{"title":"The dendritic ERGIC: Microtubule and actin cytoskeletons participate in stop-and-go movement of mobile carriers between stable structures.","authors":"María de Los Ángeles Juricic Urzúa, Javiera Gallardo Rojas, Andrés Couve Correa, Mauricio Cerda, Steffen Härtel Gründler, Carolina González-Silva","doi":"10.1111/tra.12832","DOIUrl":"https://doi.org/10.1111/tra.12832","url":null,"abstract":"<p><p>The endoplasmic reticulum (ER)-to-Golgi intermediate compartment (ERGIC) is a membranous organelle that mediates protein transport between the ER and the Golgi apparatus. In neurons, clusters of these vesiculotubular structures are situated throughout the cell in proximity to the ER, passing cargo to the cis-Golgi cisternae, located mainly in the perinuclear region. Although ERGIC markers have been identified in neurons, the distribution and dynamics of neuronal ERGIC structures have not been characterized yet. Here, we show that long-distance ERGIC transport occurs via an intermittent mechanism in dendrites, with mobile elements moving between stationary structures. Slow and fast live-cell imaging have captured stable ERGIC structures remaining in place over long periods of time, as well as mobile ERGIC structures advancing very short distances along dendrites. These short distances have been consistent with the lengths between the stationary ERGIC structures. Kymography revealed ERGIC elements that moved intermittently, emerging from and fusing with stationary ERGIC structures. Interestingly, this movement apparently depends not only on the integrity of the microtubule cytoskeleton, as previously reported, but on the actin cytoskeleton as well. Our results indicate that the dendritic ERGIC has a dual nature, with both stationary and mobile structures. The neural ERGIC network transports proteins via a stop-and-go movement in which both the microtubule and the actin cytoskeletons participate.</p>","PeriodicalId":23207,"journal":{"name":"Traffic","volume":null,"pages":null},"PeriodicalIF":4.5,"publicationDate":"2022-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39858014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}