ABC transporters: The power to change

By D. Rees, Eric F. Johnson, Oded Lewinson. Nature reviews. Molecular cell biology, 2009

1,377 citations recorded by the source corpus.

ATP-binding cassette (ABC) transporters constitute a ubiquitous superfamily of integral membrane proteins that are responsible for the ATP-powered translocation of many substrates across membranes. The highly conserved ABC domains of ABC transporters provide the nucleotide-dependent engine that drives transport. By contrast, the transmembrane domains that create the translocation pathway are more variable. Recent structural advances with prokaryotic ABC transporters have provided a qualitative molecular framework for deciphering the transport cycle. An important goal is to develop quantitative models that detail the kinetic and molecular mechanisms by which ABC transporters couple the binding and hydrolysis of ATP to substrate translocation.

Subfields: Molecular Biology, Nutrition and Dietetics, Oncology

View Paper: https://www.semanticscholar.org/paper/718a648759339ef22d48d27e1ecf5b780bc22bea

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Citations in the corpus

Overcoming ABC transporter-mediated multidrug resistance: Molecular mechanisms and novel therapeutic drug strategies. (2016, background): “In the ATP switch model, it has been proposed that drug/substrate binding to the inward facing side of the TMD promotes the switch of two NBDs from the “open” to the “closed” dimer conformation and increases the affinity to ATP (Linton, 2007; Rees et al., 2009).”
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “In spite of wide variations in their functions and substrates translocated by them, they share some common features of structure and dynamics [1435, 1436, 1437, 1438, 1439].”
Structure and mechanism of ABC transporters (2015, background): “ABC transporters classified so far can be grouped into exporters and importers with the importers further divided into two classes (I and II), depending on details of their architecture andmechanism [10-12].”
Mechanistic diversity in ATP-binding cassette (ABC) transporters (2016, background): “…glutamate, a signature LSGGQ motif that pins and orients ATP during hydrolysis, a "switch histidine" that stabilizes the transition state geometry, a Q-loop providing contacts to the TMD (not shown), and a dimerization or D-loop that has a role in coupling hydrolysis to transport (reviewed in 87 ).”
Untangling the Genetic Basis of Fibrolytic Specialization by Lachnospiraceae and Ruminococcaceae in Diverse Gut Communities (2013, background): “Regulation of ABC transporters is less well studied than for PTS; however, they are thought to be controlled by proteins acting to block specific domains [41].”
THE MECHANISM OF EUKARYOTIC TRANSLATION INITIATION AND PRINCIPLES OF ITS REGULATION (2010, background): “, unpublished observations), an essential member of the ATP-binding cassette (ABC) family of protein”
Handbook of ion channels (2015, background): “This theory is not only supported by numerous data in the literature (reviewed in Jih and Hwang, 2012), it also fits nicely with the proposed flip-flop motion of the MSD/MSD complexes that exposes the substrate binding site alternately to either side of the membrane by ATP binding–induced associatio”
Inferring interaction partners from protein sequences (2016, background): “Bacterial genomes typically contain multiple paralogs of these transporters, involved in the translocation of different substances [34].”
Inferring interaction partners from protein sequences using mutual information (2018, background): “242 First, we considered several protein pairs involved in ABC transporter complexes, which permit 243 the translocation of different substances across cell membranes [29].”