IF 4.5 3区生物学

Traffic Pub Date : 2022-03-01 Epub Date: 2022-02-02 DOI: 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":"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.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"23 3","pages":"174-187"},"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}

引用次数: 0

ERGIC2 and ERGIC3 regulate the ER-to-Golgi transport of gap junction proteins in metazoans. 在后生动物中，ERGIC2和ERGIC3调节间隙连接蛋白的ER-to-Golgi转运。

IF 4.5 3区生物学

Traffic Pub Date : 2022-03-01 Epub Date: 2022-01-26 DOI: 10.1111/tra.12830

Liying Guan, Yongzhi Yang, Jingjing Liang, Yue Miao, Angyang Shang, Baolei Wang, Yingchun Wang, Mei Ding

{"title":"ERGIC2 and ERGIC3 regulate the ER-to-Golgi transport of gap junction proteins in metazoans.","authors":"Liying Guan, Yongzhi Yang, Jingjing Liang, Yue Miao, Angyang Shang, Baolei Wang, Yingchun Wang, Mei Ding","doi":"10.1111/tra.12830","DOIUrl":"https://doi.org/10.1111/tra.12830","url":null,"abstract":"The extremely dynamic life cycle of gap junction connections requires highly efficient intracellular trafficking system especially designed for gap junction proteins, but the underlying mechanisms are largely unknown. Here, we identified that the COPII-associated proteins ERGIC2 (ER-Golgi intermediate compartment) and ERGIC3 are specifically required for the efficient intracellular transport of gap junction proteins in both Caenorhabditis elegans and mice. In the absence of Ergic2 or Ergic3, gap junction proteins accumulate in the ER and Golgi apparatus and the size of endogenous gap junction plaques is reduced. Knocking out the Ergic2 or Ergic3 in mice results in heart enlargement and cardiac malfunction accompanied by reduced number and size of connexin 43 (Cx43) gap junctions. Invertebrates' gap junction protein innexins share no sequence similarity with vertebrates' connexins. However, ERGIC2 and ERGIC3 could bind to gap junction proteins in both worms and mice. Characterization of the highly specialized roles of ERGIC2 and ERGIC3 in metazoans reveals how the early secretory pathway could be adapted to facilitate the efficient transport for gap junction proteins in vivo.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"23 3","pages":"140-157"},"PeriodicalIF":4.5,"publicationDate":"2022-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39794827","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}

引用次数: 0

Segregation of the membrane cargoes, BACE1 and amyloid precursor protein (APP) throughout the Golgi apparatus. 在整个高尔基体中膜货物，BACE1和淀粉样前体蛋白(APP)的分离。

IF 4.5 3区生物学

Traffic Pub Date : 2022-03-01 Epub Date: 2022-02-13 DOI: 10.1111/tra.12831

Lou Fourriere, Ellie Hyun-Jung Cho, Paul A Gleeson

{"title":"Segregation of the membrane cargoes, BACE1 and amyloid precursor protein (APP) throughout the Golgi apparatus.","authors":"Lou Fourriere, Ellie Hyun-Jung Cho, Paul A Gleeson","doi":"10.1111/tra.12831","DOIUrl":"https://doi.org/10.1111/tra.12831","url":null,"abstract":"The intracellular trafficking of β-site amyloid precursor protein (APP) cleaving enzyme (BACE1) and APP regulates amyloid-β production. Our previous work demonstrated that newly synthesized BACE1 and APP are segregated into distinct trafficking pathways from the trans-Golgi network (TGN), and that alterations in their trafficking lead to an increase in Aβ production in non-neuronal and neuronal cells. However, it is not known whether BACE1 and APP are transported through the Golgi stacks together and sorted at the TGN or segregated prior to arrival at the TGN. To address this question, we have used high-resolution Airyscan technology followed by Huygens deconvolution to quantify the overlap of BACE1 and APP in Golgi subcompartments in HeLa cells and primary neurons. Here, we show that APP and BACE1 are segregated, on exit from the endoplasmic reticulum and in the cis-Golgi and throughout the Golgi stack. In contrast, the transferrin receptor, which exits the TGN in AP-1 mediated transport carriers as for BACE1, colocalizes with BACE1, but not APP, throughout the Golgi stack. The segregation of APP and BACE1 is independent of the Golgi ribbon structure and the cytoplasmic domain of the cargo. Overall, our findings reveal the segregation of different membrane cargoes early in the secretory pathway, a finding relevant to the regulation of APP processing events.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"23 3","pages":"158-173"},"PeriodicalIF":4.5,"publicationDate":"2022-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9303681/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39734652","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}

引用次数: 4

Withdrawal 撤军

IF 4.5 3区生物学

Traffic Pub Date : 2022-02-12 DOI: 10.1111/tra.12837

Xiaolu Wang, Yanqiu Liu, Qian Yang, Yishun Shu, Chao Sun, L. Yin, Jian Zou, Pengfei Zhan, Yangningzhi Wang, Meili Wu, Xusheng Yang, Jiping Cai, Yong Yao, Tian-hua Xie

引用次数: 2

Bro1 binds the Vps20 subunit of ESCRT-III and promotes ESCRT-III regulation by Doa4. Bro1结合ESCRT-III的Vps20亚基，并通过Doa4促进ESCRT-III的调控。

IF 4.5 3区生物学

Traffic Pub Date : 2022-02-01 DOI: 10.1111/tra.12828

Dalton Buysse, Matt West, Mitchell Leih, Greg Odorizzi

{"title":"Bro1 binds the Vps20 subunit of ESCRT-III and promotes ESCRT-III regulation by Doa4.","authors":"Dalton Buysse, Matt West, Mitchell Leih, Greg Odorizzi","doi":"10.1111/tra.12828","DOIUrl":"https://doi.org/10.1111/tra.12828","url":null,"abstract":"The budding of intralumenal vesicles (ILVs) at endosomes requires membrane scission by the ESCRT-III complex. This step is negatively regulated in yeast by Doa4, the ubiquitin hydrolase that deubiquitinates transmembrane proteins sorted as cargoes into ILVs. Doa4 acts non-enzymatically to inhibit ESCRT-III membrane scission activity by directly binding the Snf7 subunit of ESCRT-III. This interaction inhibits the remodeling/disassembly of Snf7 polymers required for the ILV membrane scission reaction. Thus, Doa4 is thought to have a structural role that delays ILV budding while it also functions enzymatically to deubiquitinate ILV cargoes. In this study, we show that Doa4 binding to Snf7 in vivo is antagonized by another ESCRT-III subunit, Vps20. Doa4 is restricted from interacting with Snf7 in yeast expressing a mutant Vps20 allele that constitutively binds Doa4. This inhibitory effect of Vps20 is suppressed by overexpression of another ESCRT-III-associated protein, Bro1. We show that Bro1 binds directly to Vps20, suggesting that Bro1 has a central role in relieving the antagonistic relationship that Vps20 has toward Doa4.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"23 2","pages":"109-119"},"PeriodicalIF":4.5,"publicationDate":"2022-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8792227/pdf/nihms-1764596.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10601954","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}

引用次数: 1

Vps501, a novel vacuolar SNX-BAR protein cooperates with the SEA complex to regulate TORC1 signaling. 新型液泡 SNX-BAR 蛋白 Vps501 与 SEA 复合物合作调节 TORC1 信号。

IF 4.5 3区生物学

Traffic Pub Date : 2022-01-30 DOI: 10.1111/tra.12833

Shreya Goyal, Verónica A Segarra, Nitika, Aaron M Stetcher, Andrew W Truman, Adam M Reitzel, Richard J Chi

{"title":"Vps501, a novel vacuolar SNX-BAR protein cooperates with the SEA complex to regulate TORC1 signaling.","authors":"Shreya Goyal, Verónica A Segarra, Nitika, Aaron M Stetcher, Andrew W Truman, Adam M Reitzel, Richard J Chi","doi":"10.1111/tra.12833","DOIUrl":"10.1111/tra.12833","url":null,"abstract":"The sorting nexins (SNX), constitute a diverse family of molecules that play varied roles in membrane trafficking, cell signaling, membrane remodeling, organelle motility and autophagy. In particular, the SNX-BAR proteins, a SNX subfamily characterized by a C-terminal dimeric Bin/Amphiphysin/Rvs (BAR) lipid curvature domain and a conserved Phox-homology domain, are of great interest. In budding yeast, many SNX-BARs proteins have well-characterized endo-vacuolar trafficking roles. Phylogenetic analyses allowed us to identify an additional SNX-BAR protein, Vps501, with a novel endo-vacuolar role. We report that Vps501 uniquely localizes to the vacuolar membrane and has physical and genetic interactions with the SEA complex to regulate TORC1 inactivation. We found cells displayed a severe deficiency in starvation-induced/nonselective autophagy only when SEA complex subunits are ablated in combination with Vps501, indicating a cooperative role with the SEA complex during TORC1 signaling during autophagy induction. Additionally, we found the SEACIT complex becomes destabilized in vps501Δsea1Δ cells, which resulted in aberrant endosomal TORC1 activity and subsequent Atg13 hyperphosphorylation. We have also discovered that the vacuolar localization of Vps501 is dependent upon a direct interaction with Sea1 and a unique lipid binding specificity that is also required for its function. This article is protected by copyright. All rights reserved.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":" ","pages":""},"PeriodicalIF":4.5,"publicationDate":"2022-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9305297/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39874342","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}

引用次数: 0

Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum. 胶原蛋白具有独特的SEC24偏好，可以有效地从内质网输出。

IF 4.5 3区生物学

Traffic Pub Date : 2022-01-01 DOI: 10.1111/tra.12826

Chung-Ling Lu, Steven Ortmeier, Jon Brudvig, Tamara Moretti, Jacob Cain, Simeon A Boyadjiev, Jill M Weimer, Jinoh Kim

{"title":"Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum.","authors":"Chung-Ling Lu, Steven Ortmeier, Jon Brudvig, Tamara Moretti, Jacob Cain, Simeon A Boyadjiev, Jill M Weimer, Jinoh Kim","doi":"10.1111/tra.12826","DOIUrl":"https://doi.org/10.1111/tra.12826","url":null,"abstract":"SEC24 is mainly involved in cargo sorting during COPII vesicle assembly. There are four SEC24 paralogs (A-D) in vertebrates, which are classified into two subgroups (SEC24A/B and SEC24C/D). Pathological mutations in SEC24D cause osteogenesis imperfecta with craniofacial dysplasia in humans. sec24d mutant fish also recapitulate the phenotypes. Consistent with the skeletal phenotypes, the secretion of collagen was severely defective in mutant fish, emphasizing the importance of SEC24D in collagen secretion. However, SEC24D patient-derived fibroblasts show only a mild secretion phenotype, suggesting tissue-specificity in the secretion process. Using Sec24d KO mice and cultured cells, we show that SEC24A and SEC24B also contribute to endoplasmic reticulum (ER) export of procollagen. In contrast, fibronectin 1 requires either SEC24C or SEC24D for ER export. On the basis of our results, we propose that procollagen interacts with multiple SEC24 paralogs for efficient export from the ER, and that this is the basis for tissue-specific phenotypes resulting from SEC24 paralog deficiency.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"23 1","pages":"81-93"},"PeriodicalIF":4.5,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8692420/pdf/nihms-1755513.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10806062","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}

引用次数: 7

EAP45 association with budding HIV-1: Kinetics and domain requirements. EAP45与出芽HIV-1的关联:动力学和结构域要求。

IF 4.5 3区生物学

Traffic Pub Date : 2021-12-01 Epub Date: 2021-10-03 DOI: 10.1111/tra.12820

Bo Meng, Pedro P Vallejo Ramirez, Katharina M Scherer, Ezra Bruggeman, Julia C Kenyon, Clemens F Kaminski, Andrew M Lever

{"title":"EAP45 association with budding HIV-1: Kinetics and domain requirements.","authors":"Bo Meng, Pedro P Vallejo Ramirez, Katharina M Scherer, Ezra Bruggeman, Julia C Kenyon, Clemens F Kaminski, Andrew M Lever","doi":"10.1111/tra.12820","DOIUrl":"https://doi.org/10.1111/tra.12820","url":null,"abstract":"A number of viruses including HIV use the ESCRT system to bud from the infected cell. We have previously confirmed biochemically that ESCRT-II is involved in this process in HIV-1 and have defined the molecular domains that are important for this. Here, using SNAP-tag fluorescent labelling and both fixed and live cell imaging we show that the ESCRT-II component EAP45 colocalises with the HIV protein Gag at the plasma membrane in a temporal and quantitative manner, similar to that previously shown for ALIX and Gag. We show evidence that a proportion of EAP45 may be packaged within virions, and we confirm the importance of the N terminus of EAP45 and specifically the H0 domain in this process. By contrast, the Glue domain of EAP45 is more critical for recruitment during cytokinesis, emphasising that viruses have ways of recruiting cellular components that may be distinct from those used by some cellular processes. This raises the prospect of selective interference with the pathway to inhibit viral function while leaving cellular functions relatively unperturbed.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"22 12","pages":"439-453"},"PeriodicalIF":4.5,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39487518","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}

引用次数: 1

Secretion of a low-molecular-weight species of endogenous GRP94 devoid of the KDEL motif during endoplasmic reticulum stress in Chinese hamster ovary cells. 中国仓鼠卵巢细胞内质网应激过程中缺乏KDEL基序的低分子量内源性GRP94的分泌

IF 4.5 3区生物学

Traffic Pub Date : 2021-12-01 Epub Date: 2021-09-27 DOI: 10.1111/tra.12818

Andrew Samy, Noriko Yamano-Adachi, Yuichi Koga, Takeshi Omasa

{"title":"Secretion of a low-molecular-weight species of endogenous GRP94 devoid of the KDEL motif during endoplasmic reticulum stress in Chinese hamster ovary cells.","authors":"Andrew Samy, Noriko Yamano-Adachi, Yuichi Koga, Takeshi Omasa","doi":"10.1111/tra.12818","DOIUrl":"https://doi.org/10.1111/tra.12818","url":null,"abstract":"GRP94 (glucose-regulated protein 94) is a well-studied chaperone with a lysine, aspartic acid, glutamic acid and leucine (KDEL) motif at its C-terminal, which is responsible for GRP94 localization in the endoplasmic reticulum (ER). GRP94 is upregulated during ER stress to help fold unfolded proteins or direct proteins to ER-associated degradation. In a previous study, engineered GRP94 without the KDEL motif stimulated a powerful immune response in vaccine cells. In this report, we show that endogenous GRP94 is naturally secreted into the medium in a truncated form that lacks the KDEL motif in Chinese hamster ovary cells. The secretion of the truncated form of GRP94 was stimulated by the induction of ER stress. These truncations prevent GRP94 recognition by KDEL receptors and retention inside the cell. This study sheds light on a potential trafficking phenomenon during the unfolded protein response that may help understand the functional role of GRP94 as a trafficking molecule.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"22 12","pages":"425-438"},"PeriodicalIF":4.5,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5d/10/TRA-22-425.PMC9293085.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39428718","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}

引用次数: 3

A basic model for cell cholesterol homeostasis. 细胞胆固醇稳态的基本模型。

IF 4.5 3区生物学

Traffic Pub Date : 2021-12-01 Epub Date: 2021-10-19 DOI: 10.1111/tra.12816

Theodore L Steck, S M Ali Tabei, Yvonne Lange

{"title":"A basic model for cell cholesterol homeostasis.","authors":"Theodore L Steck, S M Ali Tabei, Yvonne Lange","doi":"10.1111/tra.12816","DOIUrl":"https://doi.org/10.1111/tra.12816","url":null,"abstract":"Cells manage their cholesterol by negative feedback using a battery of sterol-responsive proteins. How these activities are coordinated so as to specify the abundance and distribution of the sterol is unclear. We present a simple mathematical model that addresses this question. It assumes that almost all of the cholesterol is associated with phospholipids in stoichiometric complexes. A small fraction of the sterol is uncomplexed and thermodynamically active. It equilibrates among the organelles, setting their sterol level according to the affinity of their phospholipids. The activity of the homeostatic proteins in the cytoplasmic membranes is then set by their fractional saturation with uncomplexed cholesterol in competition with the phospholipids. The high-affinity phospholipids in the plasma membrane (PM) are filled to near stoichiometric equivalence, giving it most of the cell sterol. Notably, the affinity of the phospholipids in the endomembranes (EMs) is lower by orders of magnitude than that of the phospholipids in the PM. Thus, the small amount of sterol in the EMs rests far below stoichiometric capacity. Simulations match a variety of experimental data. The model captures the essence of cell cholesterol homeostasis, makes coherent a diverse set of experimental findings, provides a surprising prediction and suggests new experiments.","PeriodicalId":23207,"journal":{"name":"Traffic","volume":"22 12","pages":"471-481"},"PeriodicalIF":4.5,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/tra.12816","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39420977","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}

引用次数: 5

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