scholarly journals Evolutionary Analyses of ABC Transporters of Dictyostelium discoideum

2002 ◽  
Vol 1 (4) ◽  
pp. 643-652 ◽  
Author(s):  
Christophe Anjard ◽  
William F. Loomis
Keyword(s):  
Amino Acid ◽  
Dictyostelium Discoideum ◽  
Abc Transporters ◽  
Sequence Homology ◽  
Genome Project ◽  
The Other ◽  
Atp Binding ◽  
And Function ◽  
Insight Into ◽  
Atp Binding Cassette

ABSTRACT The ABC superfamily of genes is one of the largest in the genomes of both bacteria and eukaryotes. The proteins encoded by these genes all carry a characteristic 200- to 250-amino-acid ATP-binding cassette that gives them their family name. In bacteria they are mostly involved in nutrient import, while in eukaryotes many are involved in export. Seven different families have been defined in eukaryotes based on sequence homology, domain topology, and function. While only 6 ABC genes in Dictyostelium discoideum have been studied in detail previously, sequences from the well-advanced Dictyostelium genome project have allowed us to recognize 68 members of this superfamily. They have been classified and compared to animal, plant, and fungal orthologs in order to gain some insight into the evolution of this superfamily. It appears that many of the genes inferred to have been present in the ancestor of the crown organisms duplicated extensively in some but not all phyla, while others were lost in one lineage or the other.

scholarly journals Structural diversity of ABC transporters

2014 ◽  
Vol 143 (4) ◽  
pp. 419-435 ◽  
Author(s):  
Josy ter Beek ◽  
Albert Guskov ◽  
Dirk Jan Slotboom
Keyword(s):  
Abc Transporters ◽  
Transport Mechanism ◽  
Protein Complexes ◽  
Structural Characteristics ◽  
Structural Diversity ◽  
Atp Binding ◽  
Vast Array ◽  
Dependent Protein ◽  
Insight Into ◽  
Atp Binding Cassette

ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.

scholarly journals Syntaxin 17, an ancient SNARE paralog, plays different and conserved roles in different organisms

2021 ◽  
Author(s):  
Shun Kato ◽  
Kohei Arasaki ◽  
Natsuki Tokutomi ◽  
Yuzuru Imai ◽  
Tsuyoshi Inoshita ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Fusion ◽  
Basic Amino Acid ◽  
The Other ◽  
Autophagosome Formation ◽  
Hydrophobic Region ◽  
Mitochondrial Division ◽  
Eukaryotic Organisms ◽  
And Function ◽  
Insight Into

Mammalian syntaxin 17 (Stx17) has several functions, other than membrane fusion, including mitochondrial division, autophagosome formation and lipid droplet expansion. Different from conventional syntaxins, Stx17 has a long C-terminal hydrophobic region with a hairpin-like structure flanked by a basic amino acid-enriched C-terminal tail. Although Stx17 is one of the six ancient SNAREs and present in diverse eukaryotic organisms, it has been lost in multiple lineages during evolution. In the present study, we compared the localization and function of fly and nematode Stx17s expressed in HeLa cells with those of human Stx17. We found that fly Stx17 predominantly localizes to the cytosol and mediates autophagy, but not mitochondrial division. Nematode Stx17, on the other hand, is predominantly present in mitochondria and facilitates mitochondrial division, but is irrelevant to autophagy. These differences are likely due to different structures in the C-terminal tail. Non-participation of fly Stx17 and nematode Stx17 in mitochondrial division and autophagy, respectively, was demonstrated in individual organisms. Our results provide an insight into the evolution of Stx17 in metazoa.

scholarly journals Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region

1997 ◽  
Vol 323 (3) ◽  
pp. 777-783 ◽  
Author(s):  
Éva BAKOS ◽  
Izabella KLEIN ◽  
Ervin WELKER ◽  
Katalin SZABÓ ◽  
Marianna MÜLLER ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Amino Acid ◽  
Atpase Activity ◽  
Single Amino Acid ◽  
Membrane Insertion ◽  
Atp Binding ◽  
Mdr1 Expression ◽  
And Function ◽  
Atp Binding Cassette

A number of mutants with single amino acid replacements were generated in the highly conserved ATP-binding cassette (ABC)-signature region (amino acids 531–543) of the N-terminal half of the human multidrug resistance (MDR1) protein. The cDNA variants were inserted into recombinant baculoviruses and the MDR1 proteins were expressed in Spodoptera frugiperda (Sf9) insect cells. The level of expression and membrane insertion of the MDR1 variants was examined by immunostaining, and MDR1 function was followed by measuring drug-stimulated ATPase activity. We found that two mutations, L531R and G534V, practically eliminated MDR1 expression; thus these amino acid replacements seem to inhibit the formation of a stable MDR1 protein structure. The MDR1 variants G534D and I541R were expressed at normal levels with normal membrane insertion, but showed a complete loss of drug-stimulated ATPase activity, while mutant R538M yielded full protein expression but with greatly decreased ATPase activity. Increasing the ATP concentration did not restore MDR1 ATPase activity in these variants. Some amino acid replacements in the ABC-signature region (K536I, K536R, I541T and R543S) affected neither the expression and membrane insertion nor the ATPase function of MDR1. We found no alteration in the drug-sensitivity of ATP cleavage in any of the MDR1 variants that had measurable ATPase activity. These observations suggest that the ABC-signature region is essential for MDR1 protein stability and function, but alterations in this region do not seem to modulate MDR1–drug interactions directly.

Growth Promotion and Increased ATP-Binding Cassette Transporters Expression by Liraglutide in Triple Negative Breast Cancer Cell Line MDA-MB-231

Drug Research ◽  
2021 ◽  
Author(s):  
Amir Shadboorestan ◽  
Parastoo Tarighi ◽  
Mahsa Koosha ◽  
Homa Faghihi ◽  
Mohammad Hossein Ghahremani ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Line ◽  
Triple Negative Breast Cancer ◽  
Abc Transporters ◽  
Triple Negative ◽  
Epithelial Mesenchymal Transition ◽  
Growth Promotion ◽  
Atp Binding ◽  
Mesenchymal Transition ◽  
Atp Binding Cassette

Background Glucagon-like petide-1 (GLP-1) agonists such as liraglutide are widely employed in type 2 diabetes due to their glucose reducing properties and small risk of hypoglycemia. Recently, it has been shown that GLP-1agonists can inhibit breast cancer cells growth. Nonetheless, concerns are remained about liraglutide tumor promoting effects as stated by population studies. Material and Methods We evaluated the effects liraglutide on proliferation of MDA-MB-231 cells by MTT assay and then ATP-binding cassette (ABC) transporters expressions assessed by Real time PCR. Statistical comparisons were made using one-way analysis of variance followed by a post hoc Dunnett test. Results Here, we report that liraglutide can stimulate the growth of highly invasive triple negative cell line MDA-MB-231; which can be attributed to AMPK-dependent epithelial-mesenchymal transition (EMT) happening in MDA-MB-231 context. Toxicity effects were only observed with concentrations far above the serum liraglutide concentration. ATP-binding cassette (ABC) transporters expressions were upregulated, indicating the possible drug resistance and increased EMT. Conclusion In conclusion, these results suggest that liraglutide should be used with caution in patients who are suffering or have the personal history of triple negative breast cancer. However, more detailed studies are required to deepen understanding of liraglutide consequences in triple negative breast cancer. ▶Graphical Abstract.

Increased plasma plant sterol concentrations and a heterozygous amino acid exchange in ATP binding cassette transporter ABCG5: A case report

2011 ◽  
Vol 54 (4) ◽  
pp. e458-e460 ◽  
Author(s):  
Sylvia Keller ◽  
Danielle Prechtl ◽  
Charalampos Aslanidis ◽  
Uta Ceglarek ◽  
Joachim Thiery ◽  
...  
Keyword(s):  
Case Report ◽  
Amino Acid ◽  
Plant Sterol ◽  
Atp Binding ◽  
Amino Acid Exchange ◽  
Atp Binding Cassette Transporter ◽  
Acid Exchange ◽  
Plasma Plant ◽  
Atp Binding Cassette

scholarly journals Correction to: ATP binding cassette (ABC) transporters: expression and clinical value in glioblastoma

2018 ◽  
Vol 138 (3) ◽  
pp. 487-487
Author(s):  
Antonin Dréan ◽  
Shai Rosenberg ◽  
François-Xavier Lejeune ◽  
Larissa Goli ◽  
Aravindan Arun Nadaradjane ◽  
...  
Keyword(s):  
Abc Transporters ◽  
Atp Binding ◽  
Clinical Value ◽  
Atp Binding Cassette

scholarly journals Expression of some ATP-binding cassette transporters in acute myeloid leukemia

2017 ◽  
Vol 9 (4) ◽  
Author(s):  
Antonella Maria Salvia ◽  
Flavia Cuviello ◽  
Sabrina Coluzzi ◽  
Roberta Nuccorini ◽  
Immacolata Attolico ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Acute Myeloid Leukemia ◽  
Abc Transporters ◽  
Healthy Subjects ◽  
Myeloid Leukemia ◽  
Resistance Mechanisms ◽  
Atp Binding ◽  
Atp Binding Cassette Transporters ◽  
Acute Myeloid ◽  
Atp Binding Cassette

Hematopoietic cells express ATP binding cassette (ABC) transporters in relation to different degrees of differentiation. One of the known multidrug resistance mechanisms in acute myeloid leukemia (AML) is the overexpression of efflux pumps belonging to the superfamily of ABC transporters such as ABCB1, ABCG2 and ABCC1. Although several studies were carried out to correlate ABC transporters expression with drug resistance, little is known about their role as markers of diagnosis and progression of the disease. For this purpose we investigated the expression, by real-time PCR, of some ABC genes in bone marrow samples of AML patients at diagnosis and after induction therapy. At diagnosis, ABCG2 was always down-regulated, while an up regulated trend for ABCC1 was observed. After therapy the examined genes showed a different expression trend and approached the values of healthy subjects suggesting that this event could be considered as a marker of AML regression. The expression levels of some ABC transporters such as ABCC6, seems to be related to gender, age and to the presence of FLT3/ITD gene mutation.

scholarly journals Role of the ATP-Binding Cassette TransporterAbcg2in the Phenotype and Function of Cardiac Side Population Cells

2008 ◽  
Vol 103 (8) ◽  
pp. 825-835 ◽  
Author(s):  
Otmar Pfister ◽  
Angelos Oikonomopoulos ◽  
Konstantina-Ioanna Sereti ◽  
Regina L. Sohn ◽  
Darragh Cullen ◽  
...  
Keyword(s):  
Side Population ◽  
Atp Binding ◽  
Side Population Cells ◽  
And Function ◽  
Atp Binding Cassette

scholarly journals Stickleback embryos use ATP-binding cassette transporters as a buffer against exposure to maternally derived cortisol

2016 ◽  
Vol 283 (1826) ◽  
pp. 20152838 ◽  
Author(s):  
Ryan T. Paitz ◽  
Syed Abbas Bukhari ◽  
Alison M. Bell
Keyword(s):  
Abc Transporters ◽  
Gasterosteus Aculeatus ◽  
Transcriptional Response ◽  
Threespine Stickleback ◽  
Egg Laying ◽  
Atp Binding ◽  
Active Efflux ◽  
Atp Binding Cassette Transporters ◽  
Stress Influences ◽  
Atp Binding Cassette

Offspring from females that experience stressful conditions during reproduction often exhibit altered phenotypes and many of these effects are thought to arise owing to increased exposure to maternal glucocorticoids. While embryos of placental vertebrates are known to regulate exposure to maternal glucocorticoids via placental steroid metabolism, much less is known about how and whether egg-laying vertebrates can control their steroid environment during embryonic development. We tested the hypothesis that threespine stickleback ( Gasterosteus aculeatus ) embryos can regulate exposure to maternal steroids via active efflux of maternal steroids from the egg. Embryos rapidly (within 72 h) cleared intact steroids, but blocking ATP-binding cassette (ABC) transporters inhibited cortisol clearance. Remarkably, this efflux of cortisol was sufficient to prevent a transcriptional response of embryos to exogenous cortisol. Taken together, these findings suggest that, much like their placental counterparts, developing fish embryos can actively regulate their exposure to maternal cortisol. These findings highlight the fact that even in egg-laying vertebrates, the realized exposure to maternal steroids is mediated by both maternal and embryonic processes and this has important implications for understanding how maternal stress influences offspring development.

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