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Related Concept Videos

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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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Certain large, lipid-insoluble drug molecules that resemble amino acids, peptides, or glucose, require specialized carrier proteins to facilitate their diffusion across cell membranes. This transport can occur through either facilitated diffusion, which does not require energy input, or active transport, which does require energy input.
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The plasma membrane, a critical structure in cellular biology, houses an array of transporters, or carrier proteins, interspersed within its lipid bilayer. These proteins play a crucial role in solute transport through facilitated diffusion, a form of passive diffusion that uses transporters to move the molecules across the membrane.
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The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
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Interdomain communication in a homodimeric ABC transporter.

Katharina-Astrid Lindt1, Stefan Frühschulz1, Robert Tampé1

  • 1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Frankfurt, Germany.

The Journal of Biological Chemistry
|June 6, 2024
PubMed
Summary

Investigating ABC transporters, this study reveals key residues in the TAPL transporter. D278 is crucial for ATP hydrolysis and peptide transport, while R288 and D292 regulate ATPase activity and outward-facing conformations.

Keywords:
ABC transportersTAPLallosteric couplinginteraction networkinterdomain signal transmission

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • ABC transporters facilitate solute transport across cellular membranes, powered by ATP.
  • Dysfunctional ABC transporters are linked to diseases like cystic fibrosis and antibiotic resistance.
  • Interdomain communication in type IV ABC transporters remains poorly understood.

Purpose of the Study:

  • To elucidate the function of conserved charged residues in the intracytosolic loop 1 of the human lysosomal peptide transporter TAPL.
  • To investigate the role of specific residues in mediating interdomain communication and regulating transport activity.

Main Methods:

  • Site-directed mutagenesis of three conserved charged residues (D278, R288, D292) in TAPL.
  • Assays to measure peptide transport and ATPase activity of wild-type and mutant TAPL transporters.
  • Analysis of nucleotide specificity (ATP vs. GTP) for hydrolysis and transport.

Main Results:

  • D278A substitution disrupted peptide transport by inhibiting ATP hydrolysis.
  • R288A and D292A substitutions reduced peptide transport but increased basal ATPase activity.
  • R288A and D292A mutants showed altered peptide-dependent ATPase activity and hydrolyzed both ATP and GTP, unlike wild-type TAPL.

Conclusions:

  • D278 is vital for bidirectional interdomain communication via polar interactions.
  • R288 and D292 regulate ATP hydrolysis, likely by stabilizing the outward-facing transporter conformation.
  • Understanding these residues' functions advances knowledge of ABC transporter mechanisms and potential therapeutic targets.