scholarly journals ATP Binding Cassette Proteins ABCG37 and ABCG33 are required for potassium-independent cesium uptake in Arabidopsis roots

2019 ◽  
Author(s):  
Mohammad Arif Ashraf ◽  
Sayaka Kumagai ◽  
Keita Ito ◽  
Ryohei Sugita ◽  
Keitaro Tanoi ◽  
...  
Keyword(s):  
Cell Biology ◽  
Environmental Concern ◽  
Chemical Properties ◽  
Root Growth Inhibition ◽  
Atp Binding ◽  
Loss Of Function ◽  
Abc Proteins ◽  
Knock Out ◽  
Group I ◽  
Atp Binding Cassette

AbstractRadiocesium, accumulated in the soil by nuclear accidents is a major environmental concern. The transport process of cesium (Cs+) is tightly linked to the indispensable plant nutrient potassium (K+) as they both belong to the group I alkali metal with similar chemical properties. Most of the transporters that had been characterized to date as Cs+ transporters are directly or indirectly linked to K+. Using a combinatorial approach of physiology, genetics, cell biology and root uptake assay, here we identified two ATP-Binding Cassette (ABC) proteins, ABCG37 and ABCG33 as facilitators of Cs+ influx. The gain-of-function mutant of ABCG37 (abcg37-1) showed hypersensitive response to Cs+-induced root growth inhibition, while the double knock out mutant of ABCG33 and ABCG37 (abcg33-1abcg37-2) showed resistance. Single loss-of-function mutant of ABCG33 and ABCG37 did not show any alteration in Cs+ response. Short term uptake experiment with radioactive Cs+ revealed reduced Cs+ uptake in abcg33-1abgc37-2 compared with wild type in presence or absence of K+. Potassium response and content were unaffected in the double mutant background confirming that Cs+ uptake by ABCG33 and ABCG37 is independent of K+. Collectively, this work identified two ABC proteins as new Cs+ influx carriers, which act redundantly and independent of K+ uptake pathway.

Leukemic CD34+CD38- Cells Display Conserved Differential Expression of Many ATP Binding-Cassette Transporter Genes.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 1380-1380
Author(s):  
Marc H.G.P. Raaijmakers ◽  
Elke P.L.M. de Grouw ◽  
Louis T.F. van de Locht ◽  
Bert A. van der Reijden ◽  
Theo J.M. de Witte ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stem Cells ◽  
Stem Cell ◽  
Abc Transporters ◽  
Cell Biology ◽  
Cell Fraction ◽  
Atp Binding ◽  
Stem Cell Biology ◽  
Hematopoietic Stem ◽  
Atp Binding Cassette

Abstract In most cases of acute myeloid leukemia (AML) CD34+CD38− cells are considered to be stem cells, responsible for the maintenance and relapse of AML. ATP binding cassette transporters function in the extrusion of xenobiotics and chemotherapeutical compounds, and may be involved in therapy resistance. Elucidation of mechanisms conferring drug resistance to CD34+CD38− cells is essential to provide novel targets for stem cell eradication in AML. We studied gene expression of all 45 transmembrane ABC transporters (the complete ABCA, B, C, D and G family) in human hematopoietic CD34+CD38− cells and more committed CD34+CD38+ progenitor cells, from healthy donors and patients with non-hematological diseases (N=11) and AML patients (N=11). Gene expression was assessed using a novel real-time RT-PCR approach with micro fluidic cards. In normal CD34+CD38− cells 36 ABC transporters were expressed, 22 of these displayed significant higher expression in the CD34+CD38− cell fraction compared to the CD34+CD38+ cell fraction. In addition to the known stem cell transporters (ABCB1, ABCC1 and ABCG2) these differential expressed genes included many members not previously associated with stem cell biology. In AML the ABC transporter expression profile was largely conserved, including expression of all 13 known drug transporters. These data suggest an important role for many ABC transporters in hematopoietic stem cell biology. In addition, the preferential expression of a high number of drug transport related transporters predicts that broad spectrum inhibition of ABC transporters is likely to be required for CD34+38− stem cell eradication in AML. This approach will, apart from affecting the leukemic stem cells, equally affect the normal stem cells.

ATP-binding cassette (ABC) proteins in untreated acute myeloid leukemia (AML) in patients 60 years and older (CALGB 9760)

2005 ◽  
Vol 23 (16_suppl) ◽  
pp. 6551-6551
Author(s):  
M. R. Baer ◽  
J. S. Shoemaker ◽  
R. Barrier ◽  
N. W. Cuviello ◽  
K. L. O’Loughlin ◽  
...  
Keyword(s):  
Acute Myeloid Leukemia ◽  
Myeloid Leukemia ◽  
Atp Binding ◽  
Abc Proteins ◽  
Acute Myeloid ◽  
Atp Binding Cassette

scholarly journals Genome-wide analysis of ATP-binding cassette (ABC) proteins in a model legume plant, Lotus japonicus: comparison with Arabidopsis ABC protein family

DNA Research ◽  
2006 ◽  
Vol 13 (5) ◽  
pp. 205-228 ◽  
Author(s):  
Akifumi Sugiyama ◽  
Nobukazu Shitan ◽  
Shusei Sato ◽  
Yasukazu Nakamura ◽  
Satoshi Tabata ◽  
...  
Keyword(s):  
Lotus Japonicus ◽  
Protein Family ◽  
Atp Binding ◽  
Abc Proteins ◽  
Model Legume ◽  
Genome Wide Analysis ◽  
Abc Protein ◽  
Genome Wide ◽  
Legume Plant ◽  
Atp Binding Cassette

scholarly journals The Escherichia coli ATP-binding cassette (ABC) proteins

2002 ◽  
Vol 28 (1) ◽  
pp. 5-13 ◽  
Author(s):  
Kenneth J. Linton ◽  
Christopher F. Higgins
Keyword(s):  
Escherichia Coli ◽  
Atp Binding ◽  
Abc Proteins ◽  
Atp Binding Cassette

scholarly journals Evaluation of the in vitro expression of ATP binding-cassette (ABC) proteins in an Ixodes ricinus cell line exposed to ivermectin

2016 ◽  
Vol 9 (1) ◽  
Author(s):  
Carlo Mangia ◽  
Alice Vismarra ◽  
Laura Kramer ◽  
Lesley Bell-Sakyi ◽  
Daniele Porretta ◽  
...  
Keyword(s):  
Cell Line ◽  
Ixodes Ricinus ◽  
Atp Binding ◽  
Abc Proteins ◽  
In Vitro Expression ◽  
Atp Binding Cassette

scholarly journals Normal Formation of a Subset of Intestinal Granules in Caenorhabditis elegans Requires ATP-binding Cassette Transporters HAF-4 and HAF-9, Which Are Highly Homologous to Human Lysosomal Peptide Transporter TAP-Like

2009 ◽  
Vol 20 (12) ◽  
pp. 2979-2990 ◽  
Author(s):  
Hiromi Kawai ◽  
Takahiro Tanji ◽  
Hirohisa Shiraishi ◽  
Mitsuo Yamada ◽  
Ryoko Iijima ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Fluorescent Protein ◽  
Model Organism ◽  
Physiological Role ◽  
Peptide Transporter ◽  
Atp Binding ◽  
Loss Of Function ◽  
Specific Expression ◽  
Atp Binding Cassette

TAP-like (TAPL; ABCB9) is a half-type ATP-binding cassette (ABC) transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome. However, the physiological role of this transporter remains to be elucidated. Comparison of genome databases reveals that TAPL is conserved in various species from a simple model organism, Caenorhabditis elegans, to mammals. C. elegans possesses homologous TAPL genes: haf-4 and haf-9. In this study, we examined the tissue-specific expression of these two genes and analyzed the phenotypes of the loss-of-function mutants for haf-4 and haf-9 to elucidate the in vivo function of these genes. Both HAF-4 and HAF-9 tagged with green fluorescent protein (GFP) were mainly localized on the membrane of nonacidic but lysosome-associated membrane protein homologue (LMP-1)-positive intestinal granules from larval to adult stage. The mutants for haf-4 and haf-9 exhibited granular defects in late larval and young adult intestinal cells, associated with decreased brood size, prolonged defecation cycle, and slow growth. The intestinal granular phenotype was rescued by the overexpression of the GFP-tagged wild-type protein, but not by the ATP-unbound form of HAF-4. These results demonstrate that two ABC transporters, HAF-4 and HAF-9, are related to intestinal granular formation and some other physiological aspects.

scholarly journals SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator

2008 ◽  
Vol 364 (1514) ◽  
pp. 257-267 ◽  
Author(s):  
Jussi Aittoniemi ◽  
Constantina Fotinou ◽  
Tim J Craig ◽  
Heidi de Wet ◽  
Peter Proks ◽  
...  
Keyword(s):  
Ion Channel ◽  
Metabolic Regulation ◽  
Molecular Mechanisms ◽  
Neonatal Diabetes ◽  
Regulatory Subunit ◽  
Atp Binding ◽  
Congenital Hyperinsulinism ◽  
Loss Of Function ◽  
Open Probability ◽  
Atp Binding Cassette

SUR1 is an ATP-binding cassette (ABC) transporter with a novel function. In contrast to other ABC proteins, it serves as the regulatory subunit of an ion channel. The ATP-sensitive (K ATP ) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR1 subunits, and it links cell metabolism to electrical activity in many cell types. ATPase activity at the nucleotide-binding domains of SUR results in an increase in K ATP channel open probability. Conversely, ATP binding to Kir6.2 closes the channel. Metabolic regulation is achieved by the balance between these two opposing effects. Precisely how SUR1 talks to Kir6.2 remains unclear, but recent studies have identified some residues and domains that are involved in both physical and functional interactions between the two proteins. The importance of these interactions is exemplified by the fact that impaired regulation of Kir6.2 by SUR1 results in human disease, with loss-of-function SUR1 mutations causing congenital hyperinsulinism and gain-of-function SUR1 mutations leading to neonatal diabetes. This paper reviews recent data on the regulation of Kir6.2 by SUR1 and considers the molecular mechanisms by which SUR1 mutations produce disease.

The Engine of ABC Proteins

Physiology ◽  
2003 ◽  
Vol 18 (5) ◽  
pp. 191-195 ◽  
Author(s):  
Guillermo A. Altenberg
Keyword(s):  
Molecular Mechanism ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Protein Families ◽  
Abc Proteins ◽  
Substrate Transport ◽  
Binding Domains ◽  
Atp Binding Cassette

Proteins that belong to the ATP-binding cassette superfamily span from bacteria to humans and comprise one of the largest protein families. These proteins are characterized by the presence of two nucleotide-binding domains, and recent studies suggest that association and dissociation of these domains is a common basic molecular mechanism of operation that couples ATP binding/hydrolysis to substrate transport across membranes.

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