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Corrigendum. 有待纠正。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-05-01 DOI: 10.1002/1873-3468.14090
{"title":"Corrigendum.","authors":"","doi":"10.1002/1873-3468.14090","DOIUrl":"https://doi.org/10.1002/1873-3468.14090","url":null,"abstract":"","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.14090","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39013833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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
Front Cover 封面
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-05-01 DOI: 10.1002/1873-3468.13827
{"title":"Front Cover","authors":"","doi":"10.1002/1873-3468.13827","DOIUrl":"https://doi.org/10.1002/1873-3468.13827","url":null,"abstract":"","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13827","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43078997","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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
Conformational changes in the nucleotide-binding domains of P-glycoprotein induced by ATP hydrolysis. ATP水解诱导p -糖蛋白核苷酸结合域的构象变化。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-12-10 DOI: 10.1002/1873-3468.13992
Sepehr Dehghani-Ghahnaviyeh, Karan Kapoor, Emad Tajkhorshid
{"title":"Conformational changes in the nucleotide-binding domains of P-glycoprotein induced by ATP hydrolysis.","authors":"Sepehr Dehghani-Ghahnaviyeh,&nbsp;Karan Kapoor,&nbsp;Emad Tajkhorshid","doi":"10.1002/1873-3468.13992","DOIUrl":"https://doi.org/10.1002/1873-3468.13992","url":null,"abstract":"<p><p>P-glycoprotein (Pgp) is a member of the ABC transporter superfamily with high physiological importance. Pgp nucleotide-binding domains (NBDs) drive the transport cycle through ATP binding and hydrolysis. We use molecular dynamics simulations to investigate the ATP hydrolysis-induced conformational changes in NBDs. Five systems, including all possible ATP/ADP combinations in the NBDs and the APO system, are simulated. ATP/ADP exchange induces conformational changes mostly within the conserved signature motif of the NBDs, resulting in relative orientational changes in the NBDs. Nucleotide removal leads to additional orientational changes in the NBDs, allowing their dissociation. Furthermore, we capture putative hydrolysis-competent configurations in which the conserved glutamate in the Walker-B motif acts as a catalytic base capturing a water molecule likely initiating ATP hydrolysis.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13992","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38575298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 11
ABCB1/MDR1/P-gp employs an ATP-dependent twist-and-squeeze mechanism to export hydrophobic drugs. ABCB1/MDR1/P-gp通过atp依赖的扭挤机制输出疏水药物。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-12-11 DOI: 10.1002/1873-3468.14018
Atsushi Kodan, Ryota Futamata, Yasuhisa Kimura, Noriyuki Kioka, Toru Nakatsu, Hiroaki Kato, Kazumitsu Ueda
{"title":"ABCB1/MDR1/P-gp employs an ATP-dependent twist-and-squeeze mechanism to export hydrophobic drugs.","authors":"Atsushi Kodan,&nbsp;Ryota Futamata,&nbsp;Yasuhisa Kimura,&nbsp;Noriyuki Kioka,&nbsp;Toru Nakatsu,&nbsp;Hiroaki Kato,&nbsp;Kazumitsu Ueda","doi":"10.1002/1873-3468.14018","DOIUrl":"https://doi.org/10.1002/1873-3468.14018","url":null,"abstract":"<p><p>ABCB1, also called MDR1 or P-glycoprotein, exports various hydrophobic compounds and plays an essential role as a protective physiological barrier in several organs, including the brain, testis, and placenta. However, little is known about the structural mechanisms that allow ABCB1 to recognize hydrophobic compounds of diverse structures or the coupling of ATP hydrolysis to uphill substrate export. High-resolution X-ray crystal structures of the pre- and post-transport states and FRET analyses in living cells have revealed that an aromatic hydrophobic network at the top of the inner cavity is key for the conformational change in ABCB1 that is triggered by a hydrophobic substrate. ATP binding, but not hydrolysis, induces a progressive network that results in a twisting motion of the whole protein, squeezing out the substrate directly to the extracellular space. This twist-and-squeeze mechanism by which ABCB1 exports hydrophobic substrates is distinct from those of other transporters.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.14018","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38673033","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 21
ABC-F translation factors: from antibiotic resistance to immune response. ABC-F翻译因子:从抗生素耐药性到免疫应答。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-12-04 DOI: 10.1002/1873-3468.13984
Corentin R Fostier, Laura Monlezun, Farès Ousalem, Shikha Singh, John F Hunt, Grégory Boël
{"title":"ABC-F translation factors: from antibiotic resistance to immune response.","authors":"Corentin R Fostier,&nbsp;Laura Monlezun,&nbsp;Farès Ousalem,&nbsp;Shikha Singh,&nbsp;John F Hunt,&nbsp;Grégory Boël","doi":"10.1002/1873-3468.13984","DOIUrl":"https://doi.org/10.1002/1873-3468.13984","url":null,"abstract":"<p><p>Energy-dependent translational throttle A (EttA) from Escherichia coli is a paradigmatic ABC-F protein that controls the first step in polypeptide elongation on the ribosome according to the cellular energy status. Biochemical and structural studies have established that ABC-F proteins generally function as translation factors that modulate the conformation of the peptidyl transferase center upon binding to the ribosomal tRNA exit site. These factors, present in both prokaryotes and eukaryotes but not in archaea, use related molecular mechanisms to modulate protein synthesis for heterogenous purposes, ranging from antibiotic resistance and rescue of stalled ribosomes to modulation of the mammalian immune response. Here, we review the canonical studies characterizing the phylogeny, regulation, ribosome interactions, and mechanisms of action of the bacterial ABC-F proteins, and discuss the implications of these studies for the molecular function of eukaryotic ABC-F proteins, including the three human family members.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13984","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38562107","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 22
Single-molecule studies of conformational states and dynamics in the ABC importer OpuA. 单分子研究的构象状态和动力学的ABC进口OpuA。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2021-01-06 DOI: 10.1002/1873-3468.14026
Konstantinos Tassis, Ruslan Vietrov, Matthijs de Koning, Marijn de Boer, Giorgos Gouridis, Thorben Cordes
{"title":"Single-molecule studies of conformational states and dynamics in the ABC importer OpuA.","authors":"Konstantinos Tassis,&nbsp;Ruslan Vietrov,&nbsp;Matthijs de Koning,&nbsp;Marijn de Boer,&nbsp;Giorgos Gouridis,&nbsp;Thorben Cordes","doi":"10.1002/1873-3468.14026","DOIUrl":"https://doi.org/10.1002/1873-3468.14026","url":null,"abstract":"<p><p>The current model of active transport via ABC importers is mostly based on structural, biochemical and genetic data. We here establish single-molecule Förster resonance energy transfer (smFRET) assays to monitor the conformational states and heterogeneity of the osmoregulatory type I ABC importer OpuA from Lactococcus lactis. We present data probing both intradomain distances that elucidate conformational changes within the substrate-binding domain (SBD) OpuAC, and interdomain distances between SBDs or transmembrane domains. Using this methodology, we studied ligand-binding mechanisms, as well as ATP and glycine betaine dependences of conformational changes. Our work expands the scope of smFRET investigations towards a class of so far unstudied ABC importers, and paves the way for a full understanding of their transport cycle in the future.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.14026","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38706350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 7
Low oxygen tension differentially regulates the expression of placental solute carriers and ABC transporters. 低氧张力对胎盘溶质载体和ABC转运蛋白表达的调控存在差异。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-10-07 DOI: 10.1002/1873-3468.13937
Ludwik Gorczyca, Jianyao Du, Kristin M Bircsak, Xia Wen, Anna M Vetrano, Lauren M Aleksunes
{"title":"Low oxygen tension differentially regulates the expression of placental solute carriers and ABC transporters.","authors":"Ludwik Gorczyca,&nbsp;Jianyao Du,&nbsp;Kristin M Bircsak,&nbsp;Xia Wen,&nbsp;Anna M Vetrano,&nbsp;Lauren M Aleksunes","doi":"10.1002/1873-3468.13937","DOIUrl":"https://doi.org/10.1002/1873-3468.13937","url":null,"abstract":"Low oxygen concentration, or hypoxia, is an important physiological regulator of placental function including chemical disposition. Here, we compared the ability of low oxygen tension to alter the expression of solute carriers (SLC) and ABC transporters in two human placental models, namely BeWo cells and term placental explants. We found that exposure to low oxygen concentration differentially regulates transporter expression in BeWo cells, including downregulation of ENT1, OATP4A1, OCTN2, BCRP, and MRP2/3/5, and upregulation of CNT1, OAT4, OATP2B1, SERT, SOAT, and MRP1. Similar upregulation of MRP1 and downregulation of MRP5 and BCRP were observed in explants, whereas uptake transporters were decreased or unchanged. Furthermore, a screening of transcriptional regulators of transporters revealed that hypoxia leads to a decrease in the mRNA levels of aryl hydrocarbon receptor, nuclear factor erythroid 2‐related factor 2, and retinoid x receptor alpha in both human placental models. These data suggest that transporter expression is differentially regulated by oxygen concentration across experimental human placental models.","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13937","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38522451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 8
The Saccharomyces cerevisiae ABC subfamily D transporter Pxa1/Pxa2p co-imports CoASH into the peroxisome. 酿酒酵母ABC亚家族D转运体Pxa1/Pxa2p共同将CoASH导入过氧化物酶体。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-11-11 DOI: 10.1002/1873-3468.13974
Carlo W T van Roermund, Lodewijk IJlst, Alison Baker, Ronald J A Wanders, Freddie L Theodoulou, Hans R Waterham
{"title":"The Saccharomyces cerevisiae ABC subfamily D transporter Pxa1/Pxa2p co-imports CoASH into the peroxisome.","authors":"Carlo W T van Roermund,&nbsp;Lodewijk IJlst,&nbsp;Alison Baker,&nbsp;Ronald J A Wanders,&nbsp;Freddie L Theodoulou,&nbsp;Hans R Waterham","doi":"10.1002/1873-3468.13974","DOIUrl":"https://doi.org/10.1002/1873-3468.13974","url":null,"abstract":"<p><p>ATP-binding cassette (ABC) subfamily D transporters are important for the uptake of fatty acids and other beta-oxidation substrates into peroxisomes. Genetic and biochemical evidence indicates that the transporters accept fatty acyl-coenzyme A that is cleaved during the transport cycle and then re-esterified in the peroxisomal lumen. However, it is not known whether free coenzyme A (CoA) is released inside or outside the peroxisome. Here we have used Saccharomyces cerevisiae and isolated peroxisomes to demonstrate that free CoA is released in the peroxisomal lumen. Thus, ABC subfamily D transporter provide an import pathway for free CoA that controls peroxisomal CoA homeostasis and tunes metabolism according to the cell's demands.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13974","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38541542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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: 12
Generation of fully functional fluorescent fusion proteins to gain insights into ABCC6 biology. 生成全功能荧光融合蛋白，以深入了解 ABCC6 的生物学特性。
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 Epub Date: 2020-11-05 DOI: 10.1002/1873-3468.13957
Flora Szeri, Fatemeh Niaziorimi, Sylvia Donnelly, Joseph Orndorff, Koen van de Wetering
{"title":"Generation of fully functional fluorescent fusion proteins to gain insights into ABCC6 biology.","authors":"Flora Szeri, Fatemeh Niaziorimi, Sylvia Donnelly, Joseph Orndorff, Koen van de Wetering","doi":"10.1002/1873-3468.13957","DOIUrl":"10.1002/1873-3468.13957","url":null,"abstract":"<p><p>ABCC6 mediates release of ATP from hepatocytes into the blood. Extracellularly, ATP is converted into the mineralization inhibitor pyrophosphate. Consequently, inactivating mutations in ABCC6 give low plasma pyrophosphate and underlie the ectopic mineralization disorder pseudoxanthoma elasticum. How ABCC6 mediates cellular ATP release is still unknown. Fluorescent ABCC6 fusion proteins would allow mechanistic studies, but fluorophores attached to the ABCC6 N- or C-terminus result in intracellular retention and degradation. Here we describe that intramolecular introduction of fluorophores yields fully functional ABCC6 fusion proteins. A corresponding ABCC6 variant in which the catalytic glutamate of the second nucleotide binding domain was mutated, correctly routed to the plasma membrane but was inactive. Finally, N-terminal His<sup>10</sup> or FLAG tags did not affect activity of the fusion proteins, allowing their purification for biochemical characterization.</p>","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7987643/pdf/nihms-1638648.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38592541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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
Front Cover 封面
IF 3.5 4区 生物学
FEBS Letters Pub Date : 2021-03-01 DOI: 10.1002/1873-3468.13823
{"title":"Front Cover","authors":"","doi":"10.1002/1873-3468.13823","DOIUrl":"https://doi.org/10.1002/1873-3468.13823","url":null,"abstract":"","PeriodicalId":50454,"journal":{"name":"FEBS Letters","volume":null,"pages":null},"PeriodicalIF":3.5,"publicationDate":"2021-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/1873-3468.13823","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42407043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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
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